SUBI_SALTY
ID SUBI_SALTY Reviewed; 329 AA.
AC P02906;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Sulfate-binding protein;
DE Flags: Precursor;
GN Name=sbp; OrderedLocusNames=STM4063;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP PROTEIN SEQUENCE OF 20-329.
RC STRAIN=LT2;
RX PubMed=6989815; DOI=10.1016/s0021-9258(19)85539-4;
RA Isihara H., Hogg R.W.;
RT "Amino acid sequence of the sulfate-binding protein from Salmonella
RT typhimurium LT2.";
RL J. Biol. Chem. 255:4614-4618(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 246-329.
RC STRAIN=LT2;
RX PubMed=2548058; DOI=10.1111/j.1365-2958.1989.tb01806.x;
RA Garrett A.R., Johnson L.A., Beacham I.R.;
RT "Isolation, molecular characterization and expression of the ushB gene of
RT Salmonella typhimurium which encodes a membrane-bound UDP-sugar
RT hydrolase.";
RL Mol. Microbiol. 3:177-186(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=3885043; DOI=10.1038/314257a0;
RA Pflugrath J.W., Quiocho F.A.;
RT "Sulphate sequestered in the sulphate-binding protein of Salmonella
RT typhimurium is bound solely by hydrogen bonds.";
RL Nature 314:257-260(1985).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=3288756; DOI=10.1016/0022-2836(88)90341-5;
RA Pflugrath J.W., Quiocho F.A.;
RT "The 2-A resolution structure of the sulfate-binding protein involved in
RT active transport in Salmonella typhimurium.";
RL J. Mol. Biol. 200:163-180(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=8251939; DOI=10.1002/pro.5560021010;
RA He J.J., Quiocho F.A.;
RT "Dominant role of local dipoles in stabilizing uncompensated charges on a
RT sulfate sequestered in a periplasmic active transport protein.";
RL Protein Sci. 2:1643-1647(1993).
CC -!- FUNCTION: This protein specifically binds sulfate and is involved in
CC its transmembrane transport.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the prokaryotic sulfate-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL22903.1; -; Genomic_DNA.
DR EMBL; X13380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03403; BYEBT.
DR RefSeq; NP_462944.1; NC_003197.2.
DR RefSeq; WP_000758711.1; NC_003197.2.
DR PDB; 1SBP; X-ray; 1.70 A; A=20-329.
DR PDBsum; 1SBP; -.
DR AlphaFoldDB; P02906; -.
DR SMR; P02906; -.
DR STRING; 99287.STM4063; -.
DR PaxDb; P02906; -.
DR EnsemblBacteria; AAL22903; AAL22903; STM4063.
DR GeneID; 1255590; -.
DR KEGG; stm:STM4063; -.
DR PATRIC; fig|99287.12.peg.4283; -.
DR HOGENOM; CLU_055615_0_1_6; -.
DR OMA; KDFGGWK; -.
DR PhylomeDB; P02906; -.
DR BioCyc; SENT99287:STM4063-MON; -.
DR EvolutionaryTrace; P02906; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal; Sulfate transport; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:6989815"
FT CHAIN 20..329
FT /note="Sulfate-binding protein"
FT /id="PRO_0000031684"
FT CONFLICT 58
FT /note="R -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63..64
FT /note="GS -> SQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="S -> SS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="V -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="H -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 33..51
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:1SBP"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:1SBP"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:1SBP"
FT TURN 221..226
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1SBP"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:1SBP"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:1SBP"
SQ SEQUENCE 329 AA; 36540 MW; AFF24D81D758CAFD CRC64;
MKKWGVGFTL LLASTSILAK DIQLLNVSYD PTRELYEQYN KAFSAHWKQE TGDNVVIRQS
HGGSGKQATS VINGIEADVV TLALAYDVDA IAERGRIDKN WIKRLPDNSA PYTSTIVFLV
RKGNPKQIHD WNDLIKPGVS VITPNPKSSG GARWNYLAAW GYALHHNNND QAKAQDFVKA
LFKNVEVLDS GARGSTNTFV ERGIGDVLIA WENEALLATN ELGKDKFEIV TPSESILAEP
TVSVVDKVVE KKDTKAVAEA YLKYLYSPEG QEIAAKNFYR PRDADVAKKY DDAFPKLKLF
TIDEVFGGWA KAQKDHFANG GTFDQISKR
