BTUF_SALCH
ID BTUF_SALCH Reviewed; 266 AA.
AC Q57T49;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=SCH_0206;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX64112.1; -; Genomic_DNA.
DR RefSeq; WP_001539046.1; NC_006905.1.
DR AlphaFoldDB; Q57T49; -.
DR SMR; Q57T49; -.
DR EnsemblBacteria; AAX64112; AAX64112; SCH_0206.
DR KEGG; sec:SCH_0206; -.
DR HOGENOM; CLU_038034_2_5_6; -.
DR OMA; WQGINLE; -.
DR Proteomes; UP000000538; Chromosome.
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..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT CHAIN 23..266
FT /note="Vitamin B12-binding protein"
FT /id="PRO_0000003503"
FT DOMAIN 25..266
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT BINDING 50
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT BINDING 242..246
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT SITE 72
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT SITE 202
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT DISULFID 183..259
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ SEQUENCE 266 AA; 29316 MW; 1036CC0CBB87A65E CRC64;
MVKQMFRALV ALLLTLPVWL YAAPRVITLS PANTELAFAA GITPVGVSSY SDYPPEAQKI
EQVSTWQGMN LERIVAMKPD LVVAWRGGNA ERQVNQLTSL GIKVMWVDAV SIEQIADTLR
QLAAWSPQPE KAQQAAQTLL NEYAALNAEY AGKAKKRVFL QFGMNPLFTS GKGSIQHQVL
TTCGGENVFA DSRVPWPQVS REQVLARHPQ AIIVAGKAGE ILKIEQYWGN LLKIPVIPLN
SDWFERASPR IILAAKQLCN ALSQVN
