ID   BTUD_SHIF8              Reviewed;         249 AA.
AC   Q0T4R9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=SFV_1514;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF03696.1; -; Genomic_DNA.
DR   RefSeq; WP_000029466.1; NC_008258.1.
DR   AlphaFoldDB; Q0T4R9; -.
DR   SMR; Q0T4R9; -.
DR   EnsemblBacteria; ABF03696; ABF03696; SFV_1514.
DR   GeneID; 66674397; -.
DR   KEGG; sfv:SFV_1514; -.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; HHADRVW; -.
DR   BioCyc; SFLE373384:SFV_RS08460-MON; -.
DR   Proteomes; UP000000659; 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_1000083967"
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;  27111 MW;  193464EB5F777253 CRC64;
     MSIVMQLQDV AESTRLGPLS GEVRAGEILH LVGPNGAGKS TLLARMAGMT SGKGSIQFAG
     QPLEAWSATK LALHRAYLSQ QQTPPFAMPV WHYLTLHQHD KTRTELLNDV AGALALDDKL
     GRSTNQLSGG EWQRVRLAAV VLQITPQANP AGQLLLLDEP MNSLDVAQQS ALDKILSALC
     QQGLAIVMSS HDLNHTLRHA HRAWLLKGGK MLASGRREEV LTPPNLAQAY GMNFRRLDIE
     GHRMLISTI