BTUF_SHIFL
ID BTUF_SHIFL Reviewed; 266 AA.
AC Q83MD7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=SF0150, S0153;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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}.
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DR EMBL; AE005674; AAN41813.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15694.1; -; Genomic_DNA.
DR RefSeq; NP_706106.1; NC_004337.2.
DR RefSeq; WP_005053399.1; NZ_WPGW01000006.1.
DR AlphaFoldDB; Q83MD7; -.
DR SMR; Q83MD7; -.
DR STRING; 198214.SF0150; -.
DR EnsemblBacteria; AAN41813; AAN41813; SF0150.
DR EnsemblBacteria; AAP15694; AAP15694; S0153.
DR GeneID; 1024500; -.
DR KEGG; sfl:SF0150; -.
DR KEGG; sfx:S0153; -.
DR PATRIC; fig|198214.7.peg.168; -.
DR HOGENOM; CLU_038034_2_5_6; -.
DR OMA; WQGINLE; -.
DR OrthoDB; 1473468at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT CHAIN 23..266
FT /note="Vitamin B12-binding protein"
FT /id="PRO_0000003507"
FT DOMAIN 25..266
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 BINDING 242..246
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..259
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ SEQUENCE 266 AA; 29395 MW; 571F26721DCD6EA1 CRC64;
MAKSLFRALV ALSFLAPLWL NAAPRVITLS PANTELAFAA GITPVGVSSY SDYPPQAQKI
EQVSTWQGMN LERIVALKPD LVIAWRGGNA ERQVDQLASL GIKVMWVDAT SIEQIANALR
QLAPWSPQPD KAEQAAQSLL DQYVQLKAQY ADKPKKRVFL QFGINPPFTS GKESIQNQVL
EVCGGENIFK DSRVPWPQVS REQVLARSPQ AIVITGGPDQ IPKIKQYWGE QLKIPVIPLT
SDWFERASPR IILAAQQLCN ALSQVD
