entry created 2011-07-27 dataset Swiss-Prot modified 2023-02-22 version 91 accession Q46AL8 name CBIM2_METBF protein recommendedName fullName evidence 1 Putative-cobalt-transport-protein-CbiM-2 alternativeName fullName evidence 1 Energy-coupling-factor-transporter-probable-substrate-capture-protein-CbiM-2 shortName evidence 1 ECF-transporter-S-component-CbiM-2 gene name evidence 1 type primary cbiM2 name type ordered-locus Mbar_A2145 organism name type scientific Methanosarcina-barkeri-(strain-Fusaro-/-DSM-804) dbReference id 269797 type NCBI-Taxonomy lineage taxon Archaea taxon Euryarchaeota taxon Stenosarchaea-group taxon Methanomicrobia taxon Methanosarcinales taxon Methanosarcinaceae taxon Methanosarcina reference key 1 citation date 2006 first 7922 last 7931 name J.-Bacteriol. type journal-article volume 188 title The-Methanosarcina-barkeri-genome:-comparative-analysis-with-Methanosarcina-acetivorans-and-Methanosarcina-mazei-reveals-extensive-rearrangement-within-methanosarcinal-genomes. authorList person name Maeder-D.L. person name Anderson-I. person name Brettin-T.S. person name Bruce-D.C. person name Gilna-P. person name Han-C.S. person name Lapidus-A. person name Metcalf-W.W. person name Saunders-E. person name Tapia-R. person name Sowers-K.R. dbReference id 16980466 type PubMed dbReference id 10.1128/jb.00810-06 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain Fusaro-/-DSM-804 comment type function text evidence 1 Part-of-the-energy-coupling-factor-(ECF)-transporter-complex-CbiMNOQ-involved-in-cobalt-import. comment type pathway text evidence 1 Cofactor-biosynthesis;-adenosylcobalamin-biosynthesis. comment type subunit text evidence 1 Forms-an-energy-coupling-factor-(ECF)-transporter-complex-composed-of-an-ATP-binding-protein-(A-component,-CbiO),-a-transmembrane-protein-(T-component,-CbiQ)-and-2-possible-substrate-capture-proteins-(S-components,-CbiM-and-CbiN)-of-unknown-stoichimetry. comment type subcellular-location subcellularLocation location evidence 1 Cell-membrane topology evidence 1 Multi-pass-membrane-protein comment type similarity text evidence 1 Belongs-to-the-CbiM-family. dbReference id CP000099 type EMBL property type protein-sequence-ID value AAZ71074.1 property type molecule-type value Genomic_DNA dbReference id WP_011307120.1 type RefSeq property type nucleotide-sequence-ID value NC_007355.1 dbReference id Q46AL8 type AlphaFoldDB dbReference id Q46AL8 type SMR dbReference id 269797.Mbar_A2145 type STRING dbReference id AAZ71074 type EnsemblBacteria property type protein-sequence-ID value AAZ71074 property type gene-ID value Mbar_A2145 dbReference id 3626544 type GeneID dbReference id mba:Mbar_A2145 type KEGG dbReference id arCOG02248 type eggNOG property type taxonomic-scope value Archaea dbReference id CLU_052508_3_0_2 type HOGENOM dbReference id ANVFSMG type OMA dbReference id 30946at2157 type OrthoDB dbReference id UPA00148 type UniPathway dbReference id GO:0043190 type GO property type term value C:ATP-binding-cassette-(ABC)-transporter-complex property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0015087 type GO property type term value F:cobalt-ion-transmembrane-transporter-activity property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0009236 type GO property type term value P:cobalamin-biosynthetic-process property type evidence value ECO:0007669 property type project value UniProtKB-UniPathway dbReference id 1.10.1760.20 type Gene3D property type match-status value 1 dbReference id MF_01462 type HAMAP property type entry-name value CbiM property type match-status value 1 dbReference id IPR018024 type InterPro property type entry-name value CbiM dbReference id IPR002751 type InterPro property type entry-name value CbiM/NikMN dbReference id PTHR43627 type PANTHER property type match-status value 1 dbReference id PTHR43627:SF1 type PANTHER property type entry-name value COBALT-TRANSPORT-PROTEIN-CBIM property type match-status value 1 dbReference id PF01891 type Pfam property type entry-name value CbiM property type match-status value 1 dbReference id TIGR00123 type TIGRFAMs property type entry-name value cbiM property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-1003 Cell-membrane keyword id KW-0169 Cobalamin-biosynthesis keyword id KW-0170 Cobalt keyword id KW-0171 Cobalt-transport keyword id KW-0406 Ion-transport keyword id KW-0472 Membrane keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix keyword id KW-0813 Transport feature description Putative-cobalt-transport-protein-CbiM-2 id PRO_0000411159 type chain location begin position 1 end position 235 feature description Helical evidence 1 type transmembrane-region location begin position 8 end position 28 feature description Helical evidence 1 type transmembrane-region location begin position 40 end position 60 feature description Helical evidence 1 type transmembrane-region location begin position 74 end position 94 feature description Helical evidence 1 type transmembrane-region location begin position 107 end position 127 feature description Helical evidence 1 type transmembrane-region location begin position 135 end position 155 feature description Helical evidence 1 type transmembrane-region location begin position 160 end position 180 feature description Helical evidence 1 type transmembrane-region location begin position 185 end position 205 evidence key 1 type ECO:0000255 source dbReference id MF_01462 type HAMAP-Rule sequence checksum C27592AF54DCB9E6 length 235 mass 25069 modified 2005-09-13 version 1 MHIMEGYLPAIWCIVWFVVSIPVVAYGVYKLNKLVKEERGILPVLAVAGAFIFVLSSLKMPSVTGSCSHPTGTGIGAIIFGPAITAVLSTIVLIYQALFLAHGGLTTLGANVFSMGIVGPIVAYLIYKTGMKAKLNFYLIVFLAATLGDWATYIVTSTELALAFPAGDILTFGGFFSSFSKFVAIFAITQVPLAIVEGAVSALLFKYIIQAKSDLLVEMKVIGEPLVRKLRGLPA 
entry created 2011-10-19 dataset Swiss-Prot modified 2023-02-22 version 29 accession E7CLP6 name SCX2F_RHOJU protein recommendedName fullName evidence 3 Putative-beta-neurotoxin-RjAa2f organism name type scientific Rhopalurus-junceus name type common Caribbean-blue-scorpion dbReference id 419285 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Arthropoda taxon Chelicerata taxon Arachnida taxon Scorpiones taxon Buthida taxon Buthoidea taxon Buthidae taxon Rhopalurus reference evidence 8 key 1 citation date 2011 first 18 last 27 name Toxicon type journal-article volume 58 title Biochemical-and-molecular-characterization-of-the-venom-from-the-Cuban-scorpion-Rhopalurus-junceus. authorList person name Garcia-Gomez-B.I. person name Coronas-F.I. person name Restano-Cassulini-R. person name Rodriguez-R.R. person name Possani-L.D. dbReference id 21605585 type PubMed dbReference id 10.1016/j.toxicon.2011.04.011 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] source tissue evidence 8 Venom-gland comment type function text evidence 1 Beta-toxins-bind-voltage-independently-at-site-4-of-sodium-channels-(Nav)-and-shift-the-voltage-of-activation-toward-more-negative-potentials-thereby-affecting-sodium-channel-activation-and-promoting-spontaneous-and-repetitive-firing. comment type subcellular-location subcellularLocation location evidence 2 Secreted comment type tissue-specificity text evidence 7 Expressed-by-the-venom-gland. comment type domain text evidence 6 Has-the-structural-arrangement-of-an-alpha-helix-connected-to-antiparallel-beta-sheets-by-disulfide-bonds-(CS-alpha/beta). comment type similarity text evidence 4 Belongs-to-the-long-(4-C-C)-scorpion-toxin-superfamily.-Sodium-channel-inhibitor-family.-Beta-subfamily. dbReference id HM233955 type EMBL property type protein-sequence-ID value ADV16833.1 property type molecule-type value mRNA dbReference id HM233956 type EMBL property type protein-sequence-ID value ADV16834.1 property type molecule-type value mRNA dbReference id E7CLP6 type AlphaFoldDB dbReference id E7CLP6 type SMR dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0019871 type GO property type term value F:sodium-channel-inhibitor-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0090729 type GO property type term value F:toxin-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0006952 type GO property type term value P:defense-response property type evidence value ECO:0007669 property type project value InterPro dbReference id cd00107 type CDD property type entry-name value Knot1 property type match-status value 1 dbReference id 3.30.30.10 type Gene3D property type entry-name value Knottin,-scorpion-toxin-like property type match-status value 1 dbReference id IPR044062 type InterPro property type entry-name value LCN-type_CS_alpha_beta_dom dbReference id IPR003614 type InterPro property type entry-name value Scorpion_toxin-like dbReference id IPR036574 type InterPro property type entry-name value Scorpion_toxin-like_sf dbReference id IPR002061 type InterPro property type entry-name value Scorpion_toxinL/defensin dbReference id PF00537 type Pfam property type entry-name value Toxin_3 property type match-status value 1 dbReference id SM00505 type SMART property type entry-name value Knot1 property type match-status value 1 dbReference id SSF57095 type SUPFAM property type entry-name value Scorpion-toxin-like property type match-status value 1 dbReference id PS51863 type PROSITE property type entry-name value LCN_CSAB property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-1015 Disulfide-bond keyword id KW-0872 Ion-channel-impairing-toxin keyword id KW-0528 Neurotoxin keyword id KW-0964 Secreted keyword id KW-0732 Signal keyword id KW-0800 Toxin keyword id KW-0738 Voltage-gated-sodium-channel-impairing-toxin feature evidence 4 type signal-peptide location begin position 1 end position 18 feature description Putative-beta-neurotoxin-RjAa2f evidence 4 id PRO_0000413451 type chain location begin position 19 end position 90 feature description LCN-type-CS-alpha/beta evidence 5 type domain location begin position 19 end position 89 feature evidence 5 type disulfide-bond location begin position 29 end position 88 feature evidence 5 type disulfide-bond location begin position 33 end position 62 feature evidence 5 type disulfide-bond location begin position 40 end position 69 feature evidence 5 type disulfide-bond location begin position 44 end position 71 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000250 source dbReference id P15226 type UniProtKB evidence key 3 type ECO:0000250 source dbReference id Q1I176 type UniProtKB evidence key 4 type ECO:0000255 evidence key 5 type ECO:0000255 source dbReference id PRU01210 type PROSITE-ProRule evidence key 6 type ECO:0000305 evidence key 7 type ECO:0000305 source dbReference id 21605585 type PubMed evidence key 8 type ECO:0000312 source dbReference id ADV16833.1 type EMBL sequence checksum 819F3840B28669D3 length 90 mass 10009 modified 2011-03-08 precursor true version 1 MKILIFIIASFMLIGVECKEGYPMGSDGCKISCVVNNEYCKGQCSYISTQEDKKWKGSDGYCYFWGLACYCTGLPENAKVWDSKTNKCGG 
entry created 2011-10-19 dataset Swiss-Prot modified 2023-02-22 version 45 accession E3MIE2 name GATC_CAERE protein recommendedName fullName evidence 1 Glutamyl-tRNA(Gln)-amidotransferase-subunit-C,-mitochondrial shortName evidence 1 Glu-AdT-subunit-C ecNumber evidence 1 6.3.5.- gene name type ORF CRE_01088 organism name type scientific Caenorhabditis-remanei name type common Caenorhabditis-vulgaris dbReference id 31234 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Nematoda taxon Chromadorea taxon Rhabditida taxon Rhabditina taxon Rhabditomorpha taxon Rhabditoidea taxon Rhabditidae taxon Peloderinae taxon Caenorhabditis reference key 1 citation date 2007-07 db EMBL/GenBank/DDBJ-databases type submission title PCAP-assembly-of-the-Caenorhabditis-remanei-genome. authorList consortium name Caenorhabditis-remanei-Sequencing-Consortium person name Wilson-R.K. scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain PB4641 comment type function text evidence 1 Allows-the-formation-of-correctly-charged-Gln-tRNA(Gln)-through-the-transamidation-of-misacylated-Glu-tRNA(Gln)-in-the-mitochondria.-The-reaction-takes-place-in-the-presence-of-glutamine-and-ATP-through-an-activated-gamma-phospho-Glu-tRNA(Gln). comment type catalytic-activity reaction evidence 1 text ATP-+-H2O-+-L-glutamine-+-L-glutamyl-tRNA(Gln)-=-ADP-+-H(+)-+-L-glutamate-+-L-glutaminyl-tRNA(Gln)-+-phosphate dbReference id RHEA:17521 type Rhea dbReference id RHEA-COMP:9681 type Rhea dbReference id RHEA-COMP:9684 type Rhea dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:29985 type ChEBI dbReference id CHEBI:30616 type ChEBI dbReference id CHEBI:43474 type ChEBI dbReference id CHEBI:58359 type ChEBI dbReference id CHEBI:78520 type ChEBI dbReference id CHEBI:78521 type ChEBI dbReference id CHEBI:456216 type ChEBI comment type subunit text evidence 1 Subunit-of-the-heterotrimeric-GatCAB-amidotransferase-(AdT)-complex,-composed-of-A,-B-and-C-subunits. comment type subcellular-location subcellularLocation location evidence 1 Mitochondrion comment type miscellaneous text evidence 1 This-protein-may-be-expected-to-contain-an-N-terminal-transit-peptide-but-none-has-been-predicted. comment type similarity text evidence 1 Belongs-to-the-GatC-family. dbReference evidence 1 id 6.3.5.- type EC dbReference id DS268447 type EMBL property type protein-sequence-ID value EFP02374.1 property type molecule-type value Genomic_DNA dbReference id XP_003104113.1 type RefSeq property type nucleotide-sequence-ID value XM_003104065.1 dbReference id E3MIE2 type AlphaFoldDB dbReference id 31234.CRE01088 type STRING dbReference id CRE01088.1 type EnsemblMetazoa property type protein-sequence-ID value CRE01088.1 property type gene-ID value WBGene00063055 dbReference id 9802776 type GeneID dbReference id 9802776 type CTD dbReference id KOG4247 type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_105899_0_0_1 type HOGENOM dbReference id E3MIE2 type InParanoid dbReference id 3084936at2759 type OrthoDB dbReference id UP000008281 type Proteomes property type component value Unassembled-WGS-sequence dbReference id GO:0030956 type GO property type term value C:glutamyl-tRNA(Gln)-amidotransferase-complex property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0005739 type GO property type term value C:mitochondrion property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0005524 type GO property type term value F:ATP-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0050567 type GO property type term value F:glutaminyl-tRNA-synthase-(glutamine-hydrolyzing)-activity property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0070681 type GO property type term value P:glutaminyl-tRNAGln-biosynthesis-via-transamidation property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0032543 type GO property type term value P:mitochondrial-translation property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0006450 type GO property type term value P:regulation-of-translational-fidelity property type evidence value ECO:0007669 property type project value InterPro dbReference id MF_00122 type HAMAP property type entry-name value GatC property type match-status value 1 dbReference id IPR003837 type InterPro property type entry-name value Asp/Glu-ADT_csu dbReference id IPR036113 type InterPro property type entry-name value Asp/Glu-ADT_sf_sub_c dbReference id PTHR15004:SF0 type PANTHER property type entry-name value GLUTAMYL-TRNA(GLN)-AMIDOTRANSFERASE-SUBUNIT-C,-MITOCHONDRIAL property type match-status value 1 dbReference id PTHR15004 type PANTHER property type entry-name value UNCHARACTERIZED property type match-status value 1 dbReference id PF02686 type Pfam property type entry-name value Glu-tRNAGln property type match-status value 1 dbReference id SSF141000 type SUPFAM property type entry-name value Glu-tRNAGln-amidotransferase-C-subunit property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0067 ATP-binding keyword id KW-0436 Ligase keyword id KW-0496 Mitochondrion keyword id KW-0547 Nucleotide-binding keyword id KW-0648 Protein-biosynthesis keyword id KW-1185 Reference-proteome feature description Glutamyl-tRNA(Gln)-amidotransferase-subunit-C,-mitochondrial id PRO_0000413315 type chain location begin position 1 end position 198 evidence key 1 type ECO:0000255 source dbReference id MF_03149 type HAMAP-Rule sequence checksum 62B437F5D9B80734 length 198 mass 22823 modified 2011-01-11 version 1 MNRFFKIVLTSTRRASTNGSGKRKTPFEGDKVHIPDEPYNSKVRFFICFKKKLKHGIQIDESLLSEMPPIDAKLISHLERLSLVRFDSEQAVANLRNSIRMAKRLELVDVEDVEPMHTVWESQECPTFDDVEEEPLPIDKVFRNAAVRFDDFFVTPPGNVPLESNERFDLNVINKWDTIGKPVAPEAKTIRLAEGRRK 
entry created 2011-11-16 dataset Swiss-Prot modified 2023-02-22 version 55 accession E8XWL7 name AAEB_RAHSY protein recommendedName fullName evidence 1 p-hydroxybenzoic-acid-efflux-pump-subunit-AaeB shortName evidence 1 pHBA-efflux-pump-protein-B gene name evidence 1 type primary aaeB name type ordered-locus Rahaq_4004 organism name type scientific Rahnella-sp.-(strain-Y9602) dbReference id 2703885 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Gammaproteobacteria taxon Enterobacterales taxon Yersiniaceae taxon Rahnella reference key 1 citation date 2011-01 db EMBL/GenBank/DDBJ-databases type submission title Complete-sequence-of-chromosome-of-Rahnella-sp.-Y9602. authorList consortium name US-DOE-Joint-Genome-Institute person name Lucas-S. person name Copeland-A. person name Lapidus-A. person name Cheng-J.-F. person name Goodwin-L. person name Pitluck-S. person name Lu-M. person name Detter-J.C. person name Han-C. person name Tapia-R. person name Land-M. person name Hauser-L. person name Kyrpides-N. person name Ivanova-N. person name Ovchinnikova-G. person name Pagani-I. person name Sobecky-P.A. person name Martinez-R.J. person name Woyke-T. scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain Y9602 comment type function text evidence 1 Forms-an-efflux-pump-with-AaeA.-Could-function-as-a-metabolic-relief-valve,-allowing-to-eliminate-certain-compounds-when-they-accumulate-to-high-levels-in-the-cell. comment type subcellular-location subcellularLocation location evidence 1 Cell-inner-membrane topology evidence 1 Multi-pass-membrane-protein comment type similarity text evidence 1 Belongs-to-the-aromatic-acid-exporter-ArAE-(TC-2.A.85)-family. dbReference id CP002505 type EMBL property type protein-sequence-ID value ADW75592.1 property type molecule-type value Genomic_DNA dbReference id WP_013577281.1 type RefSeq property type nucleotide-sequence-ID value NC_015061.1 dbReference id E8XWL7 type AlphaFoldDB dbReference id E8XWL7 type SMR dbReference id 741091.Rahaq_4004 type STRING dbReference id ADW75592 type EnsemblBacteria property type protein-sequence-ID value ADW75592 property type gene-ID value Rahaq_4004 dbReference id rah:Rahaq_4004 type KEGG dbReference id COG1289 type eggNOG property type taxonomic-scope value Bacteria dbReference id CLU_027647_0_0_6 type HOGENOM dbReference id MITQACE type OMA dbReference id 9807111at2 type OrthoDB dbReference id UP000007257 type Proteomes property type component value Chromosome dbReference id GO:0005886 type GO property type term value C:plasma-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0022857 type GO property type term value F:transmembrane-transporter-activity property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0046942 type GO property type term value P:carboxylic-acid-transport property type evidence value ECO:0007669 property type project value InterPro dbReference id MF_01545 type HAMAP property type entry-name value AaeB property type match-status value 1 dbReference id IPR006726 type InterPro property type entry-name value PHBA_efflux_AaeB/fusaric-R dbReference id IPR023706 type InterPro property type entry-name value PHBA_efflux_pump_AaeB dbReference id PTHR30509:SF9 type PANTHER property type entry-name value MULTIDRUG-RESISTANCE-PROTEIN-MDTO property type match-status value 1 dbReference id PTHR30509 type PANTHER property type entry-name value P-HYDROXYBENZOIC-ACID-EFFLUX-PUMP-SUBUNIT-RELATED property type match-status value 1 dbReference id PF04632 type Pfam property type entry-name value FUSC property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0997 Cell-inner-membrane keyword id KW-1003 Cell-membrane keyword id KW-0472 Membrane keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix keyword id KW-0813 Transport feature description p-hydroxybenzoic-acid-efflux-pump-subunit-AaeB id PRO_0000414006 type chain location begin position 1 end position 652 feature description Helical evidence 1 type transmembrane-region location begin position 11 end position 31 feature description Helical evidence 1 type transmembrane-region location begin position 41 end position 61 feature description Helical evidence 1 type transmembrane-region location begin position 65 end position 85 feature description Helical evidence 1 type transmembrane-region location begin position 91 end position 111 feature description Helical evidence 1 type transmembrane-region location begin position 118 end position 138 feature description Helical evidence 1 type transmembrane-region location begin position 368 end position 388 feature description Helical evidence 1 type transmembrane-region location begin position 405 end position 425 feature description Helical evidence 1 type transmembrane-region location begin position 430 end position 450 feature description Helical evidence 1 type transmembrane-region location begin position 455 end position 475 feature description Helical evidence 1 type transmembrane-region location begin position 480 end position 500 evidence key 1 type ECO:0000255 source dbReference id MF_01545 type HAMAP-Rule sequence checksum 6B4E5DAB73E9B0C7 length 652 mass 71930 modified 2011-04-05 version 1 MNSVLIPRVRFACKLTFAILGALVLGFYLQLETPRWSAMTAAIVTSGPALAAGGEPFAGAIRHRGFLRVIGTFIGCIAALVIVIATARAPVVMLLLCCIWAGVCTWWSSLVRIENSYALGLAGYTALIIVVTSASSPLQTPQFAVERCSEIVIGICCAIVADLLFSPRSIKKDIDRAVSQLMLDQFALMRICVNSGTKEEIDKSWNNLVKSTTALNGMRGSLMMESSRWQRCNRRLKALHSTSLSMITQACETYLIMQSSPERVSPELKALFAEPAENVADVHRRLKQLRQMITGMHSDNVLMTVSAWTGAGTRALLLMKGIQTNSSISAIESGVLDGEVVVRPVSAERHHALVNGLRTFTATTIGCLMWLWTGWTSASGCVIIIAVVTSLAMRTPNPKGMAMDFIIGMLLAIPVGSMMFMLIMPATQQSLFLLCLMLGIFTFFIGIEVTKRRLGMLGLLAGTINILVLSNPMVFNVTSFLDNAMGQAIGTVIAMAVLLIVRDKSREKTGRTLLNRFMSSAVSALTTKAYRRRENHLPALYHQLNQLLVMFPNDIGKYRLALMLIIAHQRMKLAEVPVNDELSAFHKKIRNTADHVVSASGEGKRTYYYQRLLKELGEYQEKLVEYDAPLKVTEPVRRLTDMLQRYQHAFLA 
entry created 2011-12-14 dataset Swiss-Prot modified 2023-02-22 version 72 accession Q7DDQ4 name FTSL_NEIMB protein recommendedName fullName evidence 2 Cell-division-protein-FtsL gene name evidence 2 type primary ftsL name type ordered-locus NMB0412 organism name type scientific Neisseria-meningitidis-serogroup-B-(strain-MC58) dbReference id 122586 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Betaproteobacteria taxon Neisseriales taxon Neisseriaceae taxon Neisseria reference key 1 citation date 2000 first 1809 last 1815 name Science type journal-article volume 287 title Complete-genome-sequence-of-Neisseria-meningitidis-serogroup-B-strain-MC58. authorList person name Tettelin-H. person name Saunders-N.J. person name Heidelberg-J.F. person name Jeffries-A.C. person name Nelson-K.E. person name Eisen-J.A. person name Ketchum-K.A. person name Hood-D.W. person name Peden-J.F. person name Dodson-R.J. person name Nelson-W.C. person name Gwinn-M.L. person name DeBoy-R.T. person name Peterson-J.D. person name Hickey-E.K. person name Haft-D.H. person name Salzberg-S.L. person name White-O. person name Fleischmann-R.D. person name Dougherty-B.A. person name Mason-T.M. person name Ciecko-A. person name Parksey-D.S. person name Blair-E. person name Cittone-H. person name Clark-E.B. person name Cotton-M.D. person name Utterback-T.R. person name Khouri-H.M. person name Qin-H. person name Vamathevan-J.J. person name Gill-J. person name Scarlato-V. person name Masignani-V. person name Pizza-M. person name Grandi-G. person name Sun-L. person name Smith-H.O. person name Fraser-C.M. person name Moxon-E.R. person name Rappuoli-R. person name Venter-J.C. dbReference id 10710307 type PubMed dbReference id 10.1126/science.287.5459.1809 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain MC58 comment type function text evidence 2 Essential-cell-division-protein.-May-link-together-the-upstream-cell-division-proteins,-which-are-predominantly-cytoplasmic,-with-the-downstream-cell-division-proteins,-which-are-predominantly-periplasmic. comment type subunit text evidence 2 Part-of-a-complex-composed-of-FtsB,-FtsL-and-FtsQ. comment type subcellular-location subcellularLocation location evidence 2 Cell-inner-membrane topology evidence 2 Single-pass-type-II-membrane-protein text evidence 2 Localizes-to-the-division-septum-where-it-forms-a-ring-structure. comment type similarity text evidence 2 Belongs-to-the-FtsL-family. dbReference id AE002098 type EMBL property type protein-sequence-ID value AAF40851.1 property type molecule-type value Genomic_DNA dbReference id A81202 type PIR property type entry-name value A81202 dbReference id NP_273461.1 type RefSeq property type nucleotide-sequence-ID value NC_003112.2 dbReference id Q7DDQ4 type AlphaFoldDB dbReference id Q7DDQ4 type SMR dbReference id Q7DDQ4 type PaxDb dbReference id AAF40851 type EnsemblBacteria property type protein-sequence-ID value AAF40851 property type gene-ID value NMB0412 dbReference id nme:NMB0412 type KEGG dbReference id fig|122586.8.peg.522 type PATRIC dbReference id CLU_156524_0_2_4 type HOGENOM dbReference id DWSRLQY type OMA dbReference id 8613384at2 type OrthoDB dbReference id UP000000425 type Proteomes property type component value Chromosome dbReference id GO:0032153 type GO property type term value C:cell-division-site property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0005886 type GO property type term value C:plasma-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0043093 type GO property type term value P:FtsZ-dependent-cytokinesis property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id MF_00910 type HAMAP property type entry-name value FtsL property type match-status value 1 dbReference id IPR011922 type InterPro property type entry-name value Cell_div_FtsL dbReference id PF04999 type Pfam property type entry-name value FtsL property type match-status value 1 dbReference id TIGR02209 type TIGRFAMs property type entry-name value ftsL_broad property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0131 Cell-cycle keyword id KW-0132 Cell-division keyword id KW-0997 Cell-inner-membrane keyword id KW-1003 Cell-membrane keyword id KW-0175 Coiled-coil keyword id KW-0472 Membrane keyword id KW-1185 Reference-proteome keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description Cell-division-protein-FtsL id PRO_0000414564 type chain location begin position 1 end position 89 feature description Cytoplasmic evidence 2 type topological-domain location begin position 1 end position 6 feature description Helical evidence 2 type transmembrane-region location begin position 7 end position 24 feature description Periplasmic evidence 2 type topological-domain location begin position 25 end position 89 feature evidence 1 type coiled-coil-region location begin position 33 end position 73 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000255 source dbReference id MF_00910 type HAMAP-Rule sequence checksum 9D313BEB0929DEB5 length 89 mass 10186 modified 2004-07-05 version 1 MAMNKLNFLLLLAVCVSAFSVVMQQNQYRLNFTALDKAKKQEIALEQDYAQMRLQQARLANHEAIRAAAEKQNLHPPVSGNTFMVEHQR 
entry created 2012-05-16 dataset Swiss-Prot modified 2023-02-22 version 25 accession E6Z0R4 name VBHA_BARSR protein recommendedName fullName Antitoxin-VbhA gene name type ORF B11C_100027 organism name type scientific Bartonella-schoenbuchensis-(strain-DSM-13525-/-NCTC-13165-/-R1) dbReference id 687861 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Alphaproteobacteria taxon Hyphomicrobiales taxon Bartonellaceae taxon Bartonella reference key 1 citation date 2011 first E1001296 last E1001296 name PLoS-Genet. type journal-article volume 7 title Parallel-evolution-of-a-type-IV-secretion-system-in-radiating-lineages-of-the-host-restricted-bacterial-pathogen-Bartonella. authorList person name Engel-P. person name Salzburger-W. person name Liesch-M. person name Chang-C.C. person name Maruyama-S. person name Lanz-C. person name Calteau-A. person name Lajus-A. person name Medigue-C. person name Schuster-S.C. person name Dehio-C. dbReference id 21347280 type PubMed dbReference id 10.1371/journal.pgen.1001296 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain DSM-13525-/-NCTC-13165-/-R1 reference key 2 citation date 2012 first 107 last 110 name Nature type journal-article volume 482 title Adenylylation-control-by-intra--or-intermolecular-active-site-obstruction-in-Fic-proteins. authorList person name Engel-P. person name Goepfert-A. person name Stanger-F.V. person name Harms-A. person name Schmidt-A. person name Schirmer-T. person name Dehio-C. dbReference id 22266942 type PubMed dbReference id 10.1038/nature10729 type DOI scope X-RAY-CRYSTALLOGRAPHY-(1.5-ANGSTROMS)-OF-2-61-IN-COMPLEX-WITH-VBHT scope FUNCTION scope INTERACTION-WITH-VBHT scope MUTAGENESIS-OF-GLU-24 source strain DSM-13525-/-NCTC-13165-/-R1 comment type function text evidence 1 Antitoxin-component-of-type-II-toxin-antitoxin-(TA)-system-VbhT-VbhA.-Acts-by-inhibiting-the-adenylyltransferase-activity-of-VbhT;-competes-with-ATP-binding-and-prevents-productive-ATP-binding-to-VbhT. comment type subunit text evidence 1 Interacts-with-VbhT. comment type interaction interactant intactId EBI-15965363 id E6Z0R4 interactant intactId EBI-15965345 id E6Z0R3 label vbhT organismsDiffer false experiments 2 dbReference id FN645515 type EMBL property type protein-sequence-ID value CBI82702.1 property type molecule-type value Genomic_DNA dbReference id 3SHG type PDB property type method value X-ray property type resolution value 1.50-A property type chains value B=2-61 dbReference id 3ZC7 type PDB property type method value X-ray property type resolution value 2.10-A property type chains value B=2-62 dbReference id 3ZCB type PDB property type method value X-ray property type resolution value 1.94-A property type chains value B=1-62 dbReference id 3SHG type PDBsum dbReference id 3ZC7 type PDBsum dbReference id 3ZCB type PDBsum dbReference id E6Z0R4 type AlphaFoldDB dbReference id E6Z0R4 type SMR dbReference id DIP-60137N type DIP dbReference id E6Z0R4 type IntAct property type interactions value 1 dbReference id GO:0005524 type GO property type term value F:ATP-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:1900723 type GO property type term value P:negative-regulation-of-protein-adenylylation property type evidence value ECO:0000314 property type project value UniProtKB dbReference id cd11586 type CDD property type entry-name value VbhA_like property type match-status value 1 dbReference id 1.10.8.1050 type Gene3D property type entry-name value Antitoxin-VbhA-like property type match-status value 1 dbReference id IPR041535 type InterPro property type entry-name value VbhA dbReference id IPR033788 type InterPro property type entry-name value VbhA-like dbReference id IPR043038 type InterPro property type entry-name value VbhA_sf dbReference id PF18495 type Pfam property type entry-name value VbhA property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-0067 ATP-binding keyword id KW-0547 Nucleotide-binding keyword id KW-1277 Toxin-antitoxin-system feature description Antitoxin-VbhA id PRO_0000417550 type chain location begin position 1 end position 62 feature description Inhibitory-(S/T)XXXE(G/N)-motif type short-sequence-motif location begin position 20 end position 25 feature evidence 2 type binding-site location position position 24 ligand name ATP dbReference id CHEBI:30616 type ChEBI feature description Loss-of-antitoxin-activity-when-transfected-into-E.Coli-cells. evidence 1 type mutagenesis-site original E variation G location position position 24 feature evidence 3 type helix location begin position 4 end position 22 feature evidence 3 type turn location begin position 23 end position 25 feature evidence 3 type helix location begin position 30 end position 40 feature evidence 3 type helix location begin position 46 end position 58 evidence key 1 type ECO:0000269 source dbReference id 22266942 type PubMed evidence key 2 type ECO:0000305 evidence key 3 type ECO:0007829 source dbReference id 3SHG type PDB sequence checksum FD80CC67A913A5AF length 62 mass 7270 modified 2011-03-08 version 1 MLSEEEIEYRRRDARNALASQRLEGLEPDPQVVAQMERVVVGELETSDVIKDLMERIKREEI 
entry created 2012-09-05 dataset Swiss-Prot modified 2023-02-22 version 60 accession Q9AJE3 name CYC2_KITGR protein recommendedName fullName Terpentetriene-synthase ecNumber 4.2.3.36 gene name type primary cyc2 organism name type scientific Kitasatospora-griseola name type common Streptomyces-griseolosporeus dbReference id 2064 type NCBI-Taxonomy lineage taxon Bacteria taxon Actinobacteria taxon Streptomycetales taxon Streptomycetaceae taxon Kitasatospora reference key 1 citation date 2001 first 6085 last 6094 name J.-Bacteriol. type journal-article volume 183 title Eubacterial-diterpene-cyclase-genes-essential-for-production-of-the-isoprenoid-antibiotic-terpentecin. authorList person name Dairi-T. person name Hamano-Y. person name Kuzuyama-T. person name Itoh-N. person name Furihata-K. person name Seto-H. dbReference id 11567009 type PubMed dbReference id 10.1128/jb.183.20.6085-6094.2001 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope PATHWAY scope DISRUPTION-PHENOTYPE source strain MF730-N6 reference key 2 citation date 2002 first 37098 last 37104 name J.-Biol.-Chem. type journal-article volume 277 title Functional-analysis-of-eubacterial-diterpene-cyclases-responsible-for-biosynthesis-of-a-diterpene-antibiotic,-terpentecin. authorList person name Hamano-Y. person name Kuzuyama-T. person name Itoh-N. person name Furihata-K. person name Seto-H. person name Dairi-T. dbReference id 12138123 type PubMed dbReference id 10.1074/jbc.m206382200 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY scope COFACTOR scope BIOPHYSICOCHEMICAL-PROPERTIES scope PATHWAY scope SUBUNIT source strain MF730-N6 comment type function text evidence 2 Involved-in-the-production-of-the-isoprenoid-antibiotic-terpentecin.-Converts-terpentedienol-diphosphate-(TDP)-into-terpentetriene-(TTE).-Can-also-accept-geranylgeranyl-diphosphate-(GGDP)-and-farnesyl-diphosphate-(FDP)-as-substrates. comment type catalytic-activity reaction evidence 2 text terpentedienyl-diphosphate-=-diphosphate-+-terpentetriene dbReference id RHEA:25617 type Rhea dbReference id CHEBI:33019 type ChEBI dbReference id CHEBI:50302 type ChEBI dbReference id CHEBI:58821 type ChEBI dbReference id 4.2.3.36 type EC comment type cofactor cofactor evidence 2 name Mg(2+) dbReference id CHEBI:18420 type ChEBI comment type biophysicochemical-properties kinetics KM evidence 2 7.6-uM-for-TDP KM evidence 2 7.9-uM-for-GGDP KM evidence 2 61.7-uM-for-FDP Vmax evidence 2 114.6-nmol/min/mg-enzyme-with-TDP-as-substrate Vmax evidence 2 8.8-nmol/min/mg-enzyme-with-GGDP-as-substrate Vmax evidence 2 15.9-nmol/min/mg-enzyme-with-FDP-as-substrate phDependence text evidence 2 Optimum-pH-is-6.8. temperatureDependence text evidence 2 Optimum-temperature-is-50-degrees-Celsius. comment type pathway text evidence 1-2 Antibiotic-biosynthesis. comment type subunit text evidence 2 Homodimer. comment type disruption-phenotype text evidence 1 Mutants-do-not-produce-terpentecin. comment type similarity text evidence 3 Belongs-to-the-terpene-synthase-family. dbReference id 4.2.3.36 type EC dbReference id AB048795 type EMBL property type protein-sequence-ID value BAB39207.1 property type molecule-type value Genomic_DNA dbReference id WP_043911627.1 type RefSeq property type nucleotide-sequence-ID value NZ_JXZB01000002.1 dbReference id Q9AJE3 type AlphaFoldDB dbReference id Q9AJE3 type SMR dbReference id ag:BAB39207 type KEGG dbReference id 2989600at2 type OrthoDB dbReference id 4.2.3.36 type BRENDA property type organism-ID value 6030 dbReference id 4.2.3.B26 type BRENDA property type organism-ID value 6030 dbReference id 4.2.3.B27 type BRENDA property type organism-ID value 6030 dbReference id 4.2.3.B28 type BRENDA property type organism-ID value 6030 dbReference id 4.2.3.B29 type BRENDA property type organism-ID value 6030 dbReference id GO:0046872 type GO property type term value F:metal-ion-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0052679 type GO property type term value F:terpentetriene-synthase-activity property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0017000 type GO property type term value P:antibiotic-biosynthetic-process property type evidence value ECO:0000314 property type project value UniProtKB dbReference id cd00687 type CDD property type entry-name value Terpene_cyclase_nonplant_C1 property type match-status value 1 dbReference id 1.10.600.10 type Gene3D property type entry-name value Farnesyl-Diphosphate-Synthase property type match-status value 1 dbReference id IPR008949 type InterPro property type entry-name value Isoprenoid_synthase_dom_sf dbReference id PF19086 type Pfam property type entry-name value Terpene_syn_C_2 property type match-status value 1 dbReference id SSF48576 type SUPFAM property type entry-name value Terpenoid-synthases property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0045 Antibiotic-biosynthesis keyword id KW-0456 Lyase keyword id KW-0460 Magnesium keyword id KW-0479 Metal-binding feature description Terpentetriene-synthase id PRO_0000418818 type chain location begin position 1 end position 311 feature description DDXXD-motif type short-sequence-motif location begin position 77 end position 81 evidence key 1 type ECO:0000269 source dbReference id 11567009 type PubMed evidence key 2 type ECO:0000269 source dbReference id 12138123 type PubMed evidence key 3 type ECO:0000305 sequence checksum 7D4E9C942B6EB9A2 length 311 mass 34773 modified 2001-06-01 version 1 MPDAIEFEHEGRRNPNSAEAESAYSSIIAALDLQESDYAVISGHSRIVGAAALVYPDADAETLLAASLWTACLIVNDDRWDYVQEDGGRLAPGEWFDGVTEVVDTWRTAGPRLPDPFFELVRTTMSRLDAALGAEAADEIGHEIKRAITAMKWEGVWNEYTKKTSLATYLSFRRGYCTMDVQVVLDKWINGGRSFAALRDDPVRRAIDDVVVRFGCLSNDYYSWGREKKAVDKSNAVRILMDHAGYDESTALAHVRDDCVQAITDLDCIEESIKRSGHLGSHAQELLDYLACHRPLIYAAATWPTETNRYR 
entry created 2012-10-03 dataset Swiss-Prot modified 2023-02-22 version 35 accession P0DKB3 accession U6BY08 name MNTS_ECOLI protein recommendedName fullName Small-protein-MntS gene name type primary mntS name type synonym rybA name type ordered-locus b4705 name type ordered-locus JW0800.1 organism name type scientific Escherichia-coli-(strain-K12) dbReference id 83333 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Gammaproteobacteria taxon Enterobacterales taxon Enterobacteriaceae taxon Escherichia reference key 1 citation date 1997 first 1453 last 1462 name Science type journal-article volume 277 title The-complete-genome-sequence-of-Escherichia-coli-K-12. authorList person name Blattner-F.R. person name Plunkett-G.-III person name Bloch-C.A. person name Perna-N.T. person name Burland-V. person name Riley-M. person name Collado-Vides-J. person name Glasner-J.D. person name Rode-C.K. person name Mayhew-G.F. person name Gregor-J. person name Davis-N.W. person name Kirkpatrick-H.A. person name Goeden-M.A. person name Rose-D.J. person name Mau-B. person name Shao-Y. dbReference id 9278503 type PubMed dbReference id 10.1126/science.277.5331.1453 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain K12-/-MG1655-/-ATCC-47076 reference key 2 citation date 2006 first E1 last E5 name Mol.-Syst.-Biol. type journal-article volume 2 title Highly-accurate-genome-sequences-of-Escherichia-coli-K-12-strains-MG1655-and-W3110. authorList person name Hayashi-K. person name Morooka-N. person name Yamamoto-Y. person name Fujita-K. person name Isono-K. person name Choi-S. person name Ohtsubo-E. person name Baba-T. person name Wanner-B.L. person name Mori-H. person name Horiuchi-T. dbReference id 16738553 type PubMed dbReference id 10.1038/msb4100049 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain K12-/-W3110-/-ATCC-27325-/-DSM-5911 reference key 3 citation date 2011 first 5887 last 5897 name J.-Bacteriol. type journal-article volume 193 title The-Escherichia-coli-MntR-miniregulon-includes-genes-encoding-a-small-protein-and-an-efflux-pump-required-for-manganese-homeostasis. authorList person name Waters-L.S. person name Sandoval-M. person name Storz-G. dbReference id 21908668 type PubMed dbReference id 10.1128/jb.05872-11 type DOI scope IDENTIFICATION scope FUNCTION-IN-MANGANESE-HOMEOSTASIS scope INDUCTION scope GENE-NAME reference key 4 citation date 2011 first 32464 last 32474 name J.-Biol.-Chem. type journal-article volume 286 title Membrane-localization-of-small-proteins-in-Escherichia-coli. authorList person name Fontaine-F. person name Fuchs-R.T. person name Storz-G. dbReference id 21778229 type PubMed dbReference id 10.1074/jbc.m111.245696 type DOI scope SUBCELLULAR-LOCATION source strain K12-/-MG1655-/-ATCC-47076 comment type function text evidence 2 Required-for-repression-of-mntH-by-MntR.-May-function-as-a-chaperone-that-makes-manganese-more-available-by-delivering-it-to-the-necessary-cellular-locations-when-manganese-is-limiting. comment type subcellular-location subcellularLocation location evidence 1 Cytoplasm text May-be-loosely-associated-with-the-inner-membrane. comment type induction text evidence 2 Repressed-by-MntR-in-response-to-manganese. comment type caution text evidence 3 MntS-mRNA-was-originally-thought-to-be-an-sRNA. dbReference id U00096 type EMBL property type protein-sequence-ID value AHA50631.1 property type molecule-type value Genomic_DNA dbReference id AP009048 type EMBL property type status value NOT_ANNOTATED_CDS property type molecule-type value Genomic_DNA dbReference id WP_001001761.1 type RefSeq property type nucleotide-sequence-ID value NZ_STEB01000019.1 dbReference id YP_009029995.1 type RefSeq property type nucleotide-sequence-ID value NC_000913.3 dbReference id P0DKB3 type AlphaFoldDB dbReference id P0DKB3 type SMR dbReference id 511145.b4705 type STRING dbReference id AHA50631 type EnsemblBacteria property type protein-sequence-ID value AHA50631 property type gene-ID value b4705 dbReference id 14678509 type GeneID dbReference id 67413855 type GeneID dbReference id eco:b4705 type KEGG dbReference id fig|1411691.4.peg.1462 type PATRIC dbReference id ENOG5033AZ9 type eggNOG property type taxonomic-scope value Bacteria dbReference id 6563017at2 type OrthoDB dbReference id EcoCyc:MON0-4216 type BioCyc dbReference id PR:P0DKB3 type PRO dbReference id UP000000318 type Proteomes property type component value Chromosome dbReference id UP000000625 type Proteomes property type component value Chromosome dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0030026 type GO property type term value P:cellular-manganese-ion-homeostasis property type evidence value ECO:0000315 property type project value EcoCyc dbReference id GO:0071287 type GO property type term value P:cellular-response-to-manganese-ion property type evidence value ECO:0000270 property type project value EcoCyc proteinExistence type evidence-at-protein-level keyword id KW-0963 Cytoplasm keyword id KW-1185 Reference-proteome feature description Small-protein-MntS id PRO_0000419287 type chain location begin position 1 end position 42 evidence key 1 type ECO:0000269 source dbReference id 21778229 type PubMed evidence key 2 type ECO:0000269 source dbReference id 21908668 type PubMed evidence key 3 type ECO:0000305 sequence checksum 963F9247AFA10A2A length 42 mass 5031 modified 2012-10-03 version 1 MNEFKRCMRVFSHSPFKVRLMLLSMLCDMVNNKPQQDKPSDK 
entry created 2013-03-06 dataset Swiss-Prot modified 2023-02-22 version 54 accession Q9AGF2 name FTSX_AERHY protein recommendedName fullName evidence 1-5 Cell-division-protein-FtsX gene name evidence 5 type primary ftsX organism name type scientific Aeromonas-hydrophila dbReference id 644 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Gammaproteobacteria taxon Aeromonadales taxon Aeromonadaceae taxon Aeromonas reference evidence 4-5 key 1 citation date 2001 first 183 last 188 name FEMS-Microbiol.-Lett. type journal-article volume 198 title The-cell-division-genes-(ftsE-and-X)-of-Aeromonas-hydrophila-and-their-relationship-with-opsonophagocytosis. authorList person name Merino-S. person name Altarriba-M. person name Gavin-R. person name Izquierdo-L. person name Tomas-J.M. dbReference id 11430412 type PubMed dbReference id 10.1111/j.1574-6968.2001.tb10640.x type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope FUNCTION scope OPERON-STRUCTURE source strain evidence 3 AH-3 comment type function text evidence 1-3 Part-of-the-ABC-transporter-FtsEX-involved-in-cellular-division.-Encoded-in-an-operon-consisting-of-genes-ftsY,-ftsE-and-ftsX. comment type subunit text evidence 1 Forms-a-membrane-associated-complex-with-FtsE. comment type subcellular-location subcellularLocation location evidence 1-2 Cell-inner-membrane topology evidence 1-2 Multi-pass-membrane-protein comment type similarity text evidence 2 Belongs-to-the-ABC-4-integral-membrane-protein-family.-FtsX-subfamily. dbReference id AF334761 type EMBL property type protein-sequence-ID value AAK20882.1 property type molecule-type value Genomic_DNA dbReference id Q9AGF2 type AlphaFoldDB dbReference id Q9AGF2 type SMR dbReference id 1448139.AI20_17580 type STRING dbReference id COG2177 type eggNOG property type taxonomic-scope value Bacteria dbReference id GO:0009276 type GO property type term value C:Gram-negative-bacterium-type-cell-wall property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0005886 type GO property type term value C:plasma-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0007049 type GO property type term value P:cell-cycle property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0051301 type GO property type term value P:cell-division property type evidence value ECO:0000317 property type project value UniProtKB dbReference id 3.30.70.3040 type Gene3D property type match-status value 1 dbReference id IPR003838 type InterPro property type entry-name value ABC3_permease_dom dbReference id IPR004513 type InterPro property type entry-name value ABC_transpt_FtsX dbReference id IPR040690 type InterPro property type entry-name value FtsX_ECD dbReference id PTHR47755 type PANTHER property type entry-name value CELL-DIVISION-PROTEIN-FTSX property type match-status value 1 dbReference id PTHR47755:SF1 type PANTHER property type entry-name value CELL-DIVISION-PROTEIN-FTSX property type match-status value 1 dbReference id PF02687 type Pfam property type entry-name value FtsX property type match-status value 1 dbReference id PF18075 type Pfam property type entry-name value FtsX_ECD property type match-status value 1 dbReference id PIRSF003097 type PIRSF property type entry-name value FtsX property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0131 Cell-cycle keyword id KW-0132 Cell-division keyword id KW-0997 Cell-inner-membrane keyword id KW-1003 Cell-membrane keyword id KW-0472 Membrane keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description Cell-division-protein-FtsX id PRO_0000421700 type chain location begin position 1 end position 317 feature description Cytoplasmic evidence 1-2 type topological-domain location begin position 1 end position 39 feature description Helical evidence 2 type transmembrane-region location begin position 40 end position 60 feature description Periplasmic evidence 1-2 type topological-domain location begin position 61 end position 188 feature description Helical evidence 2 type transmembrane-region location begin position 189 end position 209 feature description Cytoplasmic evidence 1-2 type topological-domain location begin position 210 end position 241 feature description Helical evidence 2 type transmembrane-region location begin position 242 end position 262 feature description Periplasmic evidence 1-2 type topological-domain location begin position 263 end position 280 feature description Helical evidence 2 type transmembrane-region location begin position 281 end position 301 feature description Cytoplasmic evidence 1-2 type topological-domain location begin position 302 end position 317 evidence key 1 type ECO:0000250 source dbReference id P0AC30 type UniProtKB evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000269 source dbReference id 11430412 type PubMed evidence key 4 type ECO:0000305 evidence key 5 type ECO:0000312 source dbReference id AAK20882.1 type EMBL sequence checksum 3D2EA32A683AFF65 length 317 mass 35649 modified 2001-06-01 version 1 MAIVRHKQPPLRRFMMYWVDHARQAFSSLGELWRNPLASLMTLAVLGVSLALPSCFHVLLKNAEVVEGSWQTSSQISLYLRKDLPEQSILDMKQRILLYPEVESVTYMSRDEALKEFREISGFGDALDYLDSNPLPPVLSVIPDPRWQNPEGAAELLNKLNNEDGVEQGKLDLQWLTRLQGIMNLLRHTITGIAVLLLSAVLLIVGNTLRLNILNQRSEIEVLKLVGATDAFIHRPFLYTGIWFGVIGGMLAWWLTEVMVIWSEGVVNELAGLYNSNFRLVGMGAVDGINLILLGALLGLIASWFSVHRHIRDIEPS 
entry created 2013-05-01 dataset Swiss-Prot modified 2023-02-22 version 32 accession E7CY69 name APY_BIFLN protein recommendedName fullName Exo-alpha-(1->6)-L-arabinopyranosidase shortName APY ecNumber 3.2.1.- alternativeName fullName Beta-D-galactopyranosidase gene name type primary apy organism name type scientific Bifidobacterium-longum dbReference id 216816 type NCBI-Taxonomy lineage taxon Bacteria taxon Actinobacteria taxon Bifidobacteriales taxon Bifidobacteriaceae taxon Bifidobacterium reference key 1 citation date 2011 first 1097 last 1107 name J.-Appl.-Microbiol. type journal-article volume 111 title Cloning-and-characterization-of-alpha-L-arabinofuranosidase-and-bifunctional-alpha-L-arabinopyranosidase/beta-D-galactopyranosidase-from-Bifidobacterium-longum-H-1. authorList person name Lee-J.H. person name Hyun-Y.J. person name Kim-D.H. dbReference id 21851513 type PubMed dbReference id 10.1111/j.1365-2672.2011.05128.x type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope FUNCTION scope ACTIVITY-REGULATION scope BIOPHYSICOCHEMICAL-PROPERTIES scope SUBSTRATE-SPECIFICITY scope NOMENCLATURE source strain H-1 comment type function text evidence 2 Catalyzes-the-hydrolysis-of-a-non-reducing-terminal-alpha-L-arabinopyranosidic-linkage-in-ginsenoside-Rb2-(alpha-L-arabinopyranosyl-(1->6)-alpha-D-glucopyranosyl)-to-release-alpha-D-glucopyranosyl-(Rd).-It-is-not-able-to-hydrolyze-alpha-L-arabinofuranosyl-(1->6)-alpha-D-glucopyranosyl-(Rc). comment type activity-regulation text evidence 2 Completely-inhibited-by-Cu(2+)-and-activated-by-Co(2+). comment type biophysicochemical-properties kinetics KM evidence 2 0.24-mM-for-p-nitrophenyl-alpha-L-arabinopyranoside-(pNP-aL-Ap) KM evidence 2 0.26-mM-for-p-nitrophenyl-beta-D-galactopyranoside-(pNP-bD-Ga) KM evidence 2 1.33-mM-for-Rb2 Vmax evidence 2 0.21-umol/min/mg-enzyme-with-Rb2-as-substrate Vmax evidence 2 10.02-umol/min/mg-enzyme-with-pNP-aL-Ap-as-substrate Vmax evidence 2 16.5-umol/min/mg-enzyme-with-pNP-bD-Ga-as-substrate phDependence text evidence 2 Optimum-pH-is-6.8. temperatureDependence text evidence 2 Optimum-temperature-is-48-degrees-Celsius. comment type subunit text evidence 1 Homotetramer. comment type similarity text evidence 3 Belongs-to-the-glycosyl-hydrolase-3-family. dbReference id 3.2.1.- type EC dbReference id HM803112 type EMBL property type protein-sequence-ID value ADT80794.1 property type molecule-type value Genomic_DNA dbReference id E7CY69 type AlphaFoldDB dbReference id E7CY69 type SMR dbReference id GH3 type CAZy property type family-name value Glycoside-Hydrolase-Family-3 dbReference id COG1472 type eggNOG property type taxonomic-scope value Bacteria dbReference id GO:0004553 type GO property type term value F:hydrolase-activity,-hydrolyzing-O-glycosyl-compounds property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0005975 type GO property type term value P:carbohydrate-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.1700 type Gene3D property type entry-name value Glycoside-hydrolase-family-3-C-terminal-domain property type match-status value 1 dbReference id 3.20.20.300 type Gene3D property type entry-name value Glycoside-hydrolase,-family-3,-N-terminal-domain property type match-status value 1 dbReference id 2.60.40.10 type Gene3D property type entry-name value Immunoglobulins property type match-status value 1 dbReference id IPR026891 type InterPro property type entry-name value Fn3-like dbReference id IPR019800 type InterPro property type entry-name value Glyco_hydro_3_AS dbReference id IPR002772 type InterPro property type entry-name value Glyco_hydro_3_C dbReference id IPR036881 type InterPro property type entry-name value Glyco_hydro_3_C_sf dbReference id IPR001764 type InterPro property type entry-name value Glyco_hydro_3_N dbReference id IPR036962 type InterPro property type entry-name value Glyco_hydro_3_N_sf dbReference id IPR017853 type InterPro property type entry-name value Glycoside_hydrolase_SF dbReference id IPR013783 type InterPro property type entry-name value Ig-like_fold dbReference id PTHR42715 type PANTHER property type entry-name value BETA-GLUCOSIDASE property type match-status value 1 dbReference id PTHR42715:SF10 type PANTHER property type entry-name value BETA-GLUCOSIDASE-RELATED property type match-status value 1 dbReference id PF14310 type Pfam property type entry-name value Fn3-like property type match-status value 1 dbReference id PF00933 type Pfam property type entry-name value Glyco_hydro_3 property type match-status value 1 dbReference id PF01915 type Pfam property type entry-name value Glyco_hydro_3_C property type match-status value 1 dbReference id PR00133 type PRINTS property type entry-name value GLHYDRLASE3 dbReference id SM01217 type SMART property type entry-name value Fn3_like property type match-status value 1 dbReference id SSF51445 type SUPFAM property type entry-name value (Trans)glycosidases property type match-status value 1 dbReference id SSF52279 type SUPFAM property type entry-name value Beta-D-glucan-exohydrolase,-C-terminal-domain property type match-status value 1 dbReference id PS00775 type PROSITE property type entry-name value GLYCOSYL_HYDROL_F3 property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0119 Carbohydrate-metabolism keyword id KW-0326 Glycosidase keyword id KW-0378 Hydrolase feature description Exo-alpha-(1->6)-L-arabinopyranosidase id PRO_0000422132 type chain location begin position 1 end position 757 feature evidence 1 type active-site location position position 232 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000269 source dbReference id 21851513 type PubMed evidence key 3 type ECO:0000305 sequence checksum D30956BDB329A3FE length 757 mass 81473 modified 2011-03-08 version 1 MSESTYPSVKDLTLEEKASLTSGGDAWHLQGVESKGIPSYMITDGPHGLRKSLASSAGETDLDDSVPATCFPPAAGLSSSWNPELIHKVGEAMAEECIQEKVAVILGPGVNIKRNPLGGRCFEYWSEDPYLAGHEAIGIVEGVQSKGVGTSLKHFAANNQETDRLRVDARISPRALREIYFPAFEHIVKKAQPWTIMCSYNRINGVHSAQNHWLLTDVLRDEWGFDGIVMSDWGADHDRGASLNAGLNLEMPPSYTDDQIVYAVRDGLITPAQLDRMAQGMIDLVNKTRAAMSIDNYRFDVDAHDEVAHQAAIESIVMLKNDDAILPLNAGPVANPSATPQKIAVIGEFARTPRYQGGGSSHITPTKMTSFLDTLAERGIKADFAPGFTLDLEPADPALESEAVETAKNADVVLMFLGLPEAVESEGFDRDTLDMPAKQIALLEQVAAANQNVVVVLSNGSVITVAPWAKNAKGILESWLLGQSGGPALADVIFGQVSPSGKLAQSIPLDINDDPSMLNWPGEEGHVDYGEGVFAGYRYYDTYGKAVDYPFGYGLSYATFEITGVAVAKTGANTATVTATVTNTSDVDAAETVQVYVVPGKADVARPKHELKGFTKAFLKAGESKTVAIDLDERAFAYWSEKYNDWHVEAGEYAIEVGVSSRDIADTVAVALDGDGKTQPLTEWSTYGEWEADPFGAKIVAAVAAAGEAGELTKLPDNAMMRMFLNPMPINSLPTLLGEGGKKIAQFMLDEYAKLSK 
