ID   BTUF_VIBCM              Reviewed;         276 AA.
AC   C3LQF3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=VCM66_2304;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001233; ACP06605.1; -; Genomic_DNA.
DR   RefSeq; WP_000960255.1; NC_012578.1.
DR   AlphaFoldDB; C3LQF3; -.
DR   SMR; C3LQF3; -.
DR   EnsemblBacteria; ACP06605; ACP06605; VCM66_2304.
DR   KEGG; vcm:VCM66_2304; -.
DR   HOGENOM; CLU_038034_2_5_6; -.
DR   OMA; WQGINLE; -.
DR   Proteomes; UP000001217; Chromosome I.
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; 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_1000148778"
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