BTUD_ECO8A
ID BTUD_ECO8A Reviewed; 249 AA.
AC B7M1B8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=ECIAI1_1765;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAQ98622.1; -; Genomic_DNA.
DR RefSeq; WP_000029466.1; NC_011741.1.
DR AlphaFoldDB; B7M1B8; -.
DR SMR; B7M1B8; -.
DR GeneID; 66674397; -.
DR KEGG; ecr:ECIAI1_1765; -.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; HHADRVW; -.
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_1000134661"
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