ID   BTUF_VIBPA              Reviewed;         275 AA.
AC   Q87SE7;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=VP0477;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC58740.1; -; Genomic_DNA.
DR   RefSeq; NP_796856.1; NC_004603.1.
DR   AlphaFoldDB; Q87SE7; -.
DR   SMR; Q87SE7; -.
DR   STRING; 223926.28805460; -.
DR   PRIDE; Q87SE7; -.
DR   EnsemblBacteria; BAC58740; BAC58740; BAC58740.
DR   KEGG; vpa:VP0477; -.
DR   PATRIC; fig|223926.6.peg.454; -.
DR   eggNOG; COG0614; Bacteria.
DR   HOGENOM; CLU_038034_2_5_6; -.
DR   OMA; WQGINLE; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   CHAIN           20..275
FT                   /note="Vitamin B12-binding protein"
FT                   /id="PRO_0000003509"
FT   DOMAIN          25..272
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            74
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            204
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   DISULFID        185..265
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ   SEQUENCE   275 AA;  31148 MW;  11904F3957195D92 CRC64;
     MMNKICLYLP LFFSSLTMAN EPVERVISLA PHATEIAYAA GLGDKLIAVS EMSDYPKEAG
     ELEKVSNYQG IKLERIIALQ PDLVIAWPAG NPAKELEKLK QFGVPIYYST TGTLEDIANN
     IEQLSQYSDD PSKGQKAARD FREELTALKA KYNTTEKVRY FYQLSEKPII TVAGKNWPSE
     VFNFCGGENV FANTAAPYPQ VSIEQVITRQ PEVLFTSRHA MSDDGMWAQW KNELPALRNN
     HVWSLNSDWI NRPTPRTLNA IIEVCEHFES VKRKR