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BTUD_VIBVY
ID   BTUD_VIBVY              Reviewed;         254 AA.
AC   Q7MLE6;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Vitamin B12 import ATP-binding protein BtuD {ECO:0000255|HAMAP-Rule:MF_01005};
DE            EC=7.6.2.8 {ECO:0000255|HAMAP-Rule:MF_01005};
DE   AltName: Full=Vitamin B12-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01005};
GN   Name=btuD {ECO:0000255|HAMAP-Rule:MF_01005}; OrderedLocusNames=VV1481;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex BtuCDF involved in
CC       vitamin B12 import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-
CC         cob(III)alamin(in) + H(+) + phosphate; Xref=Rhea:RHEA:17873,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:140785, ChEBI:CHEBI:456216;
CC         EC=7.6.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01005};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BtuD),
CC       two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).
CC       {ECO:0000255|HAMAP-Rule:MF_01005}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01005}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01005}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Vitamin B12
CC       importer (TC 3.A.1.13.1) family. {ECO:0000255|HAMAP-Rule:MF_01005}.
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DR   EMBL; BA000037; BAC94245.1; -; Genomic_DNA.
DR   RefSeq; WP_011150120.1; NC_005139.1.
DR   AlphaFoldDB; Q7MLE6; -.
DR   SMR; Q7MLE6; -.
DR   STRING; 672.VV93_v1c13910; -.
DR   EnsemblBacteria; BAC94245; BAC94245; BAC94245.
DR   KEGG; vvy:VV1481; -.
DR   PATRIC; fig|196600.6.peg.1466; -.
DR   eggNOG; COG4138; Bacteria.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; HHADRVW; -.
DR   OrthoDB; 1752365at2; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01005; BtuD; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR023693; ABC_transptr_BtuD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..254
FT                   /note="Vitamin B12 import ATP-binding protein BtuD"
FT                   /id="PRO_0000091964"
FT   DOMAIN          1..239
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
FT   BINDING         29..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
SQ   SEQUENCE   254 AA;  27831 MW;  1A8869CC570D3534 CRC64;
     MHINHISVGN RLLPLSFQCA AGEKVYVAGP NGSGKSTLLS AIAGTLSSRE GVKGEVLINE
     TSLLTLPLAE QAIYRAYLCQ QSRPAFNVDV FQMLALSLPA GRHVVEPEVQ AAVRRVVELV
     QLQDKLHRSV QALSGGEWQR VRLAAVCLQV WRSLNPYSQL LILDEPAAPL DVAQAKWLYQ
     LIDEMAAQGL VVIVANHDLN RVYQHADKVL LLNQGVLTAY GSADEVMSVE NLQQVFETPV
     KKVAVDGQPY LIFT
 
 
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