BTUF_PECAS
ID BTUF_PECAS Reviewed; 279 AA.
AC Q6D1Z3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=ECA3304;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG76202.1; -; Genomic_DNA.
DR RefSeq; WP_011094821.1; NC_004547.2.
DR AlphaFoldDB; Q6D1Z3; -.
DR SMR; Q6D1Z3; -.
DR STRING; 218491.ECA3304; -.
DR EnsemblBacteria; CAG76202; CAG76202; ECA3304.
DR GeneID; 57209994; -.
DR KEGG; eca:ECA3304; -.
DR PATRIC; fig|218491.5.peg.3352; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_2_5_6; -.
DR OMA; WQGINLE; -.
DR OrthoDB; 1473468at2; -.
DR Proteomes; UP000007966; 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; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT CHAIN 21..279
FT /note="Vitamin B12-binding protein"
FT /id="PRO_0000003500"
FT DOMAIN 24..276
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 208
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT DISULFID 189..265
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ SEQUENCE 279 AA; 30923 MW; 1A3395B02BA8C188 CRC64;
MTFRFLCWLT GLLLCTAAYA IPQRVISLAP HATEMAYAAG MGEQLIAVSA WSDYPPEAKK
LEQVASWQGI NLERILALKP DLILAWREGN PQRPLEQLAN FSIPIVYLDA KTLDDIPASL
RQLATYSRHP EQAERAATDF QQQIGELQHA DEKHKAAHTA PLRVFIQFGT QPLFTSSKAT
LQSQIVSLCG AENIFSDSTV PWPQVSREQV LRRQPQAIII GGASDKIANT QAFWQPQLTV
PVITVNEDWF SRSGPRLLLA AQQICSQLAE LKLAPSSAK