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 27-MAR-2024, entry version 61.
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; Pseudomonadota; 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 KEGG; vcm:VCM66_2304; -.
DR HOGENOM; CLU_038034_2_5_6; -.
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 CDD; cd01144; BtuF; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR HAMAP; MF_01000; BtuF; 1.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR InterPro; IPR023544; ABC_transptr_vit_B12-bd.
DR NCBIfam; NF038402; TroA_like; 1.
DR PANTHER; PTHR42860; VITAMIN B12-BINDING PROTEIN; 1.
DR PANTHER; PTHR42860:SF1; VITAMIN B12-BINDING PROTEIN; 1.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 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
//
