ID   BTUF_PECCP              Reviewed;         276 AA.
AC   C6DC28;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=PC1_3099;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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}.
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DR   EMBL; CP001657; ACT14122.1; -; Genomic_DNA.
DR   RefSeq; WP_015841268.1; NC_012917.1.
DR   AlphaFoldDB; C6DC28; -.
DR   SMR; C6DC28; -.
DR   STRING; 561230.PC1_3099; -.
DR   EnsemblBacteria; ACT14122; ACT14122; PC1_3099.
DR   KEGG; pct:PC1_3099; -.
DR   eggNOG; COG0614; Bacteria.
DR   HOGENOM; CLU_038034_2_5_6; -.
DR   OMA; WQGINLE; -.
DR   OrthoDB; 1473468at2; -.
DR   Proteomes; UP000002736; 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..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   CHAIN           21..276
FT                   /note="Vitamin B12-binding protein"
FT                   /id="PRO_5000485903"
FT   DOMAIN          24..273
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            73
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            205
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   DISULFID        186..262
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ   SEQUENCE   276 AA;  30386 MW;  BFC647DC109EA5C5 CRC64;
     MIVRFLCWLT GLLLCTAAYA LPQRVISLAP HATEMAYAAG MGEQLIAVSA WSDYPPEAKK
     LEQVASWQGI NLERILALKP DLILAWREGN PQRPLEQLAN FSIPIVYLDA KTLDDIPASL
     RQLATYSRHP EQAERAATDF QQEIGRLRHT GEGQNAASLR VFIQFGTQPL FTSSQATLQS
     QIVSLCGAEN IFSDSPVPWP QVSREQVLRR QPQAIIIGGS PDKIASVQTF WQPQLAVPVI
     TVNEDWFSRS GPRLLLAAQQ ICSQLTALSP GSSSAK