ID   BTUD_ECODH              Reviewed;         249 AA.
AC   B1XG16;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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};
GN   OrderedLocusNames=ECDH10B_1845;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB02910.1; -; Genomic_DNA.
DR   RefSeq; WP_000029474.1; NC_010473.1.
DR   AlphaFoldDB; B1XG16; -.
DR   SMR; B1XG16; -.
DR   KEGG; ecd:ECDH10B_1845; -.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; HHADRVW; -.
DR   BioCyc; ECOL316385:ECDH10B_RS09445-MON; -.
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_1000134662"
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;  27081 MW;  760004A5C0134245 CRC64;
     MSIVMQLQDV AESTRLGPLS GEVRAGEILH LVGPNGAGKS TLLARMAGMT SGKGSIQFAG
     QPLEAWSATK LALHRAYLSQ QQTPPFATPV WHYLTLHQHD KTRTELLNDV AGALALDDKL
     GRSTNQLSGG EWQRVRLAAV VLQITPQANP AGQLLLLDEP MNSLDVAQQS ALDKILSALC
     QQGLAIVMSS HDLNHTLRHA HRAWLLKGGK MLASGRREEV LTPPNLAQAY GMNFRRLDIE
     GHRMLISTI