BTUF_PHOPR
ID BTUF_PHOPR Reviewed; 274 AA.
AC Q6LUR6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=PBPRA0536;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378664; CAG18959.1; -; Genomic_DNA.
DR RefSeq; WP_011217312.1; NC_006370.1.
DR AlphaFoldDB; Q6LUR6; -.
DR SMR; Q6LUR6; -.
DR STRING; 298386.PBPRA0536; -.
DR EnsemblBacteria; CAG18959; CAG18959; PBPRA0536.
DR KEGG; ppr:PBPRA0536; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_2_5_6; -.
DR OMA; WQGINLE; -.
DR OrthoDB; 1473468at2; -.
DR Proteomes; UP000000593; 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..17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT CHAIN 18..274
FT /note="Vitamin B12-binding protein"
FT /id="PRO_0000003502"
FT DOMAIN 23..270
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT BINDING 50
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT SITE 72
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT SITE 202
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT DISULFID 183..263
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ SEQUENCE 274 AA; 30590 MW; 6835F92618F7177E CRC64;
MRFIYLFIAL FSSFSIAQQP ALRVISLSPH TTELAYAAGL GDALIAASDY SDYPEAAQKL
ERVANYRGVK LERIVALQPD LILAWKGGNP PREMAKLEQL GLNVFYSNPV ELEDIATTIE
QLGQYSPEPT QAIQTANQFR QEISAFKTRN ENQRTVSFFY QLSDSPIITV ADGSWPSQVF
SLCGGRNIFG DSPAAYPQVS EEQVVVRQPE VIFGTPHADT KTSIWQNWQG KLPAVDNHHV
FTLQADWLNR PTPRTINAIK QVCGLFDQVR DGTL
