ID   SUBI_SHIFL              Reviewed;         329 AA.
AC   P0AG79; P06997;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Sulfate-binding protein;
DE   AltName: Full=Sulfate starvation-induced protein 2;
DE            Short=SSI2;
DE   Flags: Precursor;
GN   Name=sbp; OrderedLocusNames=SF3995, S3752;
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: This protein specifically binds sulfate and is involved in
CC       its transmembrane transport. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic sulfate-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN45429.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18771.1; -; Genomic_DNA.
DR   RefSeq; NP_709722.1; NC_004337.2.
DR   RefSeq; WP_001045689.1; NZ_WPGW01000012.1.
DR   AlphaFoldDB; P0AG79; -.
DR   SMR; P0AG79; -.
DR   STRING; 198214.SF3995; -.
DR   EnsemblBacteria; AAN45429; AAN45429; SF3995.
DR   EnsemblBacteria; AAP18771; AAP18771; S3752.
DR   GeneID; 1025163; -.
DR   GeneID; 66672175; -.
DR   KEGG; sfl:SF3995; -.
DR   KEGG; sfx:S3752; -.
DR   PATRIC; fig|198214.7.peg.4708; -.
DR   HOGENOM; CLU_055615_0_1_6; -.
DR   OMA; KDFGGWK; -.
DR   OrthoDB; 1111285at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:1901681; F:sulfur compound binding; IEA:InterPro.
DR   GO; GO:1902358; P:sulfate transmembrane transport; IEA:InterPro.
DR   CDD; cd01005; PBP2_CysP; 1.
DR   InterPro; IPR000957; Sulphate/thiosulphate-bd_CS.
DR   InterPro; IPR034408; Sulphate/thiosulphate_BS.
DR   InterPro; IPR005669; Thiosulph/SO4-bd.
DR   PANTHER; PTHR30368; PTHR30368; 1.
DR   TIGRFAMs; TIGR00971; 3a0106s03; 1.
DR   PROSITE; PS00401; PROK_SULFATE_BIND_1; 1.
DR   PROSITE; PS00757; PROK_SULFATE_BIND_2; 1.
PE   3: Inferred from homology;
KW   Periplasm; Reference proteome; Signal; Sulfate transport; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..329
FT                   /note="Sulfate-binding protein"
FT                   /id="PRO_0000045265"
SQ   SEQUENCE   329 AA;  36659 MW;  3353D36DE484C814 CRC64;
     MNKWGVGLTF LLAATSVMAK DIQLLNVSYD PTRELYEQYN KAFSAHWKQQ TGDNVVIRQS
     HGGSGKQATS VINGIEADVV TLALAYDVDA IAERGRIDKE WIKRLPDNSA PYTSTIVFLV
     RKGNPKQIHD WNDLIKPGVS VITPNPKSSG GARWNYLAAW GYALHHNNND QAKAQDFVRA
     LYKNVEVLDS GARGSTNTFV ERGIGDVLIA WENEALLAAN ELGKDKFEIV TPSESILAEP
     TVSVVDKVVE KKGTKEVAEA YLKYLYSPEG QEIAAKNYYR PRDAEVAKKY ENAFPKLKLF
     TIDEEFGGWT KAQKEHFANG GTFDQISKR