ID   BTUF_VIBC1              Reviewed;         275 AA.
AC   A7MXP0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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};
GN   OrderedLocusNames=VIBHAR_00921;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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; CP000789; ABU69920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7MXP0; -.
DR   SMR; A7MXP0; -.
DR   EnsemblBacteria; ABU69920; ABU69920; VIBHAR_00921.
DR   KEGG; vha:VIBHAR_00921; -.
DR   PATRIC; fig|338187.25.peg.1700; -.
DR   OMA; WQGINLE; -.
DR   Proteomes; UP000008152; Chromosome I.
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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   CHAIN           20..275
FT                   /note="Vitamin B12-binding protein"
FT                   /id="PRO_1000062722"
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;  30783 MW;  65693228F3C737A4 CRC64;
     MMNKLCFALP LIFSDASFAN GPAQRIISLA PHSTEIAYSA GLGDKLIAVS EMSDYPEQAK
     DLEKVSNYQG IKLERIIALQ PDLVIAWPAG NPAKELEKLE QFGIPIYYST TGTLEGIATN
     IEQLSQYSEK PEVGQKAAAE FRAQLEALKE KYNTEDKVSY FYQLSEKPII TVAGKNWPSE
     VFTFCGGENI FSKGSAPYPQ VSIEQVITRQ PEVLFASRHA MSNDGMWAEW KNDIPALGNN
     HVWSLNSDWI NRPTSRTLNA ITEVCEHFET VRQKR