ID   SUBI_SYNE7              Reviewed;         350 AA.
AC   P27366; Q31MK8;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Sulfate-binding protein;
DE   Flags: Precursor;
GN   Name=sbpA; OrderedLocusNames=Synpcc7942_1681;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1708375; DOI=10.1128/jb.173.9.2739-2750.1991;
RA   Laudenbach D.E., Grossman A.R.;
RT   "Characterization and mutagenesis of sulfur-regulated genes in a
RT   cyanobacterium: evidence for function in sulfate transport.";
RL   J. Bacteriol. 173:2739-2750(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein specifically binds sulfate and is involved in
CC       its transmembrane transport.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: By sulfur deprivation.
CC   -!- SIMILARITY: Belongs to the prokaryotic sulfate-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; M65247; AAA73043.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57711.1; -; Genomic_DNA.
DR   RefSeq; WP_011378139.1; NC_007604.1.
DR   AlphaFoldDB; P27366; -.
DR   SMR; P27366; -.
DR   STRING; 1140.Synpcc7942_1681; -.
DR   PRIDE; P27366; -.
DR   EnsemblBacteria; ABB57711; ABB57711; Synpcc7942_1681.
DR   KEGG; syf:Synpcc7942_1681; -.
DR   eggNOG; COG1613; Bacteria.
DR   HOGENOM; CLU_055615_0_1_3; -.
DR   OMA; KDFGGWK; -.
DR   OrthoDB; 1111285at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1681-MON; -.
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   2: Evidence at transcript level;
KW   Periplasm; Signal; Stress response; Sulfate transport; Transport.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..350
FT                   /note="Sulfate-binding protein"
FT                   /id="PRO_0000031685"
SQ   SEQUENCE   350 AA;  37750 MW;  6BE33DD9203792E4 CRC64;
     MKTAWTRRSF LQSAALATAT VITIAACGGN NQSSSGGSGQ PVEVTLVSYA VTQAAYEQII
     PKFAAQWKEK TGQEVRFNQS YGGSGSQTRA VIDGLEADVV ALALESDINQ IEKAGLIQPG
     WQQRVPNNGI ITNSVVALVT QEGNPKGIKD WTDLTKPGVR IVTANPKTSG GARWNFLGAW
     GSVTQTGGTE EQALQFTTDI YKNVPILAKD ARESTDVFTK GQADVLLNYE NELILAQQKG
     EKVDYAIPPV NINIQGPVAV VDTYTDKHGT RKVSEAFVQF LFTPEAQAEF AKVGFRPALP
     EGVDPQLLAP FPKIQTWFTV ADLGGWAKVQ PEFFGDGGWF DKVQQAVAGR