BTUD_VIBC1
ID BTUD_VIBC1 Reviewed; 255 AA.
AC A7MVV6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=VIBHAR_02133;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000789; ABU71098.1; -; Genomic_DNA.
DR AlphaFoldDB; A7MVV6; -.
DR SMR; A7MVV6; -.
DR EnsemblBacteria; ABU71098; ABU71098; VIBHAR_02133.
DR KEGG; vha:VIBHAR_02133; -.
DR PATRIC; fig|338187.25.peg.559; -.
DR OMA; HHADRVW; -.
DR Proteomes; UP000008152; 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; Translocase; Transport.
FT CHAIN 1..255
FT /note="Vitamin B12 import ATP-binding protein BtuD"
FT /id="PRO_1000083970"
FT DOMAIN 2..240
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01005"
SQ SEQUENCE 255 AA; 27883 MW; 6E94170DF5B26CA2 CRC64;
MMHVKHIALG SRLLPLSFAC NPSEVVHVVG PNGSGKSTLL GAISGTLTQR EGVSGQVLVD
SNDLLTMPLS EQAHIRGYLC QQSRPTFNVD VFQYLALSLP TGANISDAKV RDAVNIVIEL
VQLQDKLHRS IQTLSGGEWQ RVRLAGVCLQ VWRTINPYSQ LLILDEPAAP LDIAQEGLLY
QLINAVAAQG IGVLVANHDL NRTLRYADKV LLLNNGVLHS LGHADEVLTE EGLAEVFQTQ
VRKVVLEDRP YLIFD
