ID   BTUF_YERPS              Reviewed;         280 AA.
AC   Q66EE7;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=YPTB0746;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19986.1; -; Genomic_DNA.
DR   RefSeq; WP_011191763.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66EE7; -.
DR   SMR; Q66EE7; -.
DR   EnsemblBacteria; CAH19986; CAH19986; YPTB0746.
DR   GeneID; 66842833; -.
DR   KEGG; yps:YPTB0746; -.
DR   OMA; WQGINLE; -.
DR   Proteomes; UP000001011; 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..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   CHAIN           28..280
FT                   /note="Vitamin B12-binding protein"
FT                   /id="PRO_0000003513"
FT   DOMAIN          30..277
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   BINDING         57
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            79
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            209
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   DISULFID        190..266
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ   SEQUENCE   280 AA;  30841 MW;  5335075B56CB9B4E CRC64;
     MMPLGLFPLP RAAVVLLISL LTLPAQAAER VISLSPSTTE LAYAAGLGDK LVAVSAYSDY
     PESAKKLEHV ASWQGINVER ILALKPDLIL AWRGGNPQRP LDQLAALGIP IFYSDPTHID
     QIASDLDKLA QYSPHPEQAH QAAEQFRQHV NTLRDRYARS QPKRTFLQFG TQPLFTSSGH
     TLQSEVVSLC GGENIFADSR VPWPQVSREQ VMTRKPQVIV VSGTQSQVDN VSAFWLPQLV
     VPVIALNEDW FNRASPRILL AAQQLCQQMA SIPTPVAESH