BTUF_VIBC3
ID BTUF_VIBC3 Reviewed; 276 AA.
AC A5F5P5; C3M4A4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
GN OrderedLocusNames=VC0395_A1959, VC395_2496;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
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; CP000627; ABQ22132.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10486.1; -; Genomic_DNA.
DR RefSeq; WP_000960255.1; NZ_JAACZH010000008.1.
DR PDB; 5YSC; X-ray; 1.67 A; A=21-276.
DR PDBsum; 5YSC; -.
DR AlphaFoldDB; A5F5P5; -.
DR SMR; A5F5P5; -.
DR STRING; 345073.VC395_2496; -.
DR EnsemblBacteria; ABQ22132; ABQ22132; VC0395_A1959.
DR KEGG; vco:VC0395_A1959; -.
DR KEGG; vcr:VC395_2496; -.
DR PATRIC; fig|345073.21.peg.2400; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_2_5_6; -.
DR OMA; WQGINLE; -.
DR BRENDA; 7.6.2.8; 15862.
DR Proteomes; UP000000249; Chromosome 2.
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 1: Evidence at protein level;
KW 3D-structure; 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_1000072889"
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"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5YSC"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 133..153
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:5YSC"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5YSC"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:5YSC"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5YSC"
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
