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BTUF_SALTY
ID   BTUF_SALTY              Reviewed;         266 AA.
AC   Q8ZRP7; Q9ZFP9;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Vitamin B12-binding protein;
DE   Flags: Precursor;
GN   Name=btuF; OrderedLocusNames=STM0206;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=10464235; DOI=10.1128/jb.181.17.5539-5541.1999;
RA   Van Bibber M., Bradbeer C., Clark N., Roth J.R.;
RT   "A new class of cobalamin transport mutants (btuF) provides genetic
RT   evidence for a periplasmic binding protein in Salmonella typhimurium.";
RL   J. Bacteriol. 181:5539-5541(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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 (By similarity). {ECO:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BtuF family. {ECO:0000305}.
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DR   EMBL; AF096877; AAC98382.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19170.1; -; Genomic_DNA.
DR   RefSeq; NP_459211.1; NC_003197.2.
DR   RefSeq; WP_001118843.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRP7; -.
DR   SMR; Q8ZRP7; -.
DR   STRING; 99287.STM0206; -.
DR   TCDB; 3.A.1.13.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q8ZRP7; -.
DR   EnsemblBacteria; AAL19170; AAL19170; STM0206.
DR   GeneID; 1251724; -.
DR   KEGG; stm:STM0206; -.
DR   PATRIC; fig|99287.12.peg.219; -.
DR   HOGENOM; CLU_038034_2_5_6; -.
DR   OMA; WQGINLE; -.
DR   PhylomeDB; Q8ZRP7; -.
DR   BioCyc; SENT99287:STM0206-MON; -.
DR   Proteomes; UP000001014; 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; Reference proteome; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..266
FT                   /note="Vitamin B12-binding protein"
FT                   /id="PRO_0000003506"
FT   DOMAIN          25..266
FT                   /note="Fe/B12 periplasmic-binding"
FT   BINDING         50
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000250"
FT   BINDING         242..246
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000250"
FT   SITE            72
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000250"
FT   SITE            202
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000250"
FT   DISULFID        183..259
FT                   /evidence="ECO:0000250"
FT   CONFLICT        149
FT                   /note="E -> Q (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="A -> P (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="R -> H (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="S -> N (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="T -> A (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="G -> W (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198..200
FT                   /note="QVS -> HVI (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="A -> G (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="Q -> H (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218..224
FT                   /note="AGEILKI -> TVGNQRY (in Ref. 1; AAC98382)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   266 AA;  29284 MW;  E08D0EFA813E2729 CRC64;
     MAKQMFRALV ALLLTLPVWL YAAPRVITLS PANTELAFAA GITPVGVSSY SDYPPEAQKI
     EQVSTWQGMN LERIVALKPD LVVAWRGGNA ERQVNQLTSL GIKVMWVDAV TIEQIADTLR
     QLAAWSPQPE KAQQAAQTLL NEYAALNAEY AGKAKKRVFL QFGMNPLFTS GKGSIQHQVL
     TTCGGENVFA DSRVPWPQVS REQVLARHPQ AIIVAGKAGE ILKIEQYWGN LLKIPVIPLN
     SDWFERASPR IILAAKQLCN ALSQVN
 
 
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