BTUF_VIBCH
ID BTUF_VIBCH Reviewed; 276 AA.
AC Q9KPI6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Vitamin B12-binding protein {ECO:0000255|HAMAP-Rule:MF_01000};
DE Flags: Precursor;
GN Name=btuF {ECO:0000255|HAMAP-Rule:MF_01000}; OrderedLocusNames=VC_2381;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Part of the ABC transporter complex BtuCDF involved in
CC vitamin B12 import. Binds vitamin B12 and delivers it to the
CC periplasmic surface of BtuC. {ECO:0000255|HAMAP-Rule:MF_01000}.
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_01000}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01000}.
CC -!- SIMILARITY: Belongs to the BtuF family. {ECO:0000255|HAMAP-
CC Rule:MF_01000}.
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DR EMBL; AE003852; AAF95524.1; -; Genomic_DNA.
DR PIR; C82084; C82084.
DR RefSeq; NP_232011.1; NC_002505.1.
DR RefSeq; WP_000960255.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KPI6; -.
DR SMR; Q9KPI6; -.
DR STRING; 243277.VC_2381; -.
DR DNASU; 2613050; -.
DR EnsemblBacteria; AAF95524; AAF95524; VC_2381.
DR KEGG; vch:VC_2381; -.
DR PATRIC; fig|243277.26.peg.2267; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_2_5_6; -.
DR OMA; WQGINLE; -.
DR BioCyc; VCHO:VC2381-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0015889; P:cobalamin transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01000; BtuF; 1.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR InterPro; IPR023544; ABC_transptr_vit_B12-bd.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT CHAIN 21..276
FT /note="Vitamin B12-binding protein"
FT /id="PRO_0000003508"
FT DOMAIN 27..274
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT BINDING 54
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT SITE 76
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT SITE 206
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT DISULFID 187..267
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ SEQUENCE 276 AA; 31071 MW; 8DA4DD66BB742AE1 CRC64;
MLVIRLIACT FLFITPSLLA KPFPAERIIS LAPHATEIAY AAGLGDKLVA VSEYSDYPPQ
ALELERVANH QTINIEKILT LKPDLIIAWP AGNPPRELAK LRQLGFTIYD SQTKTLDEIA
DNIEALSHYS ANPEVGQKAA HDFRQRLQDL RTQYASNQPI RYFYQLSEKP IITLAQGHWP
SEVFSLCGGV NIFADSEVPY PQVSIEQVLV KQPQVIFTSE HAIANGHMWR AWQAELSAVQ
NDQVWALNAD WLNRPTPRTL DAVEQVCTYL KIAQKQ