ID   BTUF_YERPY              Reviewed;         280 AA.
AC   B1JK18;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, 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=YPK_3455;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000950; ACA69722.1; -; Genomic_DNA.
DR   RefSeq; WP_012304565.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JK18; -.
DR   SMR; B1JK18; -.
DR   EnsemblBacteria; ACA69722; ACA69722; YPK_3455.
DR   KEGG; ypy:YPK_3455; -.
DR   OMA; WQGINLE; -.
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_5000315802"
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;  8B36CF6E31CB93A0 CRC64;
     MMPLGLFPLP RAAAVLLISL LTLPAQAAER VISLSPSTTE LAYAAGLGDK LVAVSAYSDY
     PESAKKLEHV ASWQGINVER ILALKPDLIL AWRGGNPQRP LDQLAALGIP IFYSDPTHID
     QIASDLDKLA QYSPHPEQAH QAAEQFRQHV NTLRDRYARS QPKRTFLQFG TQPLFTSSGH
     TLQSEVVSLC GGENIFADSR VPWPQVSRER VMTRKPQVIV VSGTQSQVDN VSAFWLPQLV
     VPVIALNEDW FNRASPRILL AAQQLCQQMA SIPTPVAESH