ID   BTUD_ECOK1              Reviewed;         249 AA.
AC   A1ABP5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Ecok1_15910;
GN   ORFNames=APECO1_784;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ01085.1; -; Genomic_DNA.
DR   RefSeq; WP_000029464.1; NC_008563.1.
DR   AlphaFoldDB; A1ABP5; -.
DR   SMR; A1ABP5; -.
DR   EnsemblBacteria; ABJ01085; ABJ01085; APECO1_784.
DR   KEGG; ecv:APECO1_784; -.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; HHADRVW; -.
DR   Proteomes; UP000008216; Chromosome.
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; IPR017871; ABC_transporter-like_CS.
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; PS00211; ABC_TRANSPORTER_1; 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; Translocase; Transport.
FT   CHAIN           1..249
FT                   /note="Vitamin B12 import ATP-binding protein BtuD"
FT                   /id="PRO_1000083961"
FT   DOMAIN          1..233
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
SQ   SEQUENCE   249 AA;  27085 MW;  192475EA5F777253 CRC64;
     MSIVMQLQDV AESTRLGPLS GEVRAGEILH LVGPNGAGKS TLLARMAGMT SGKGSIQFAG
     QPLEAWSATK LALHRAYLSQ QQTPPFAMPV WHYLTLHQHD KTRTELLNDV AGALALDDKL
     GRSTNQLSGG EWQRVRLAAV VLQITPQANP AGQLLLLDEP MNSLDVAQQS ALDKILSALC
     QQGLAIVMSS HDLNHTLRHA HRAWLLKGGK MLASGRREEV LTPANLAQAY GMNFRRLDIE
     GHRMLISTI