HSPQ_SALTI
ID HSPQ_SALTI Reviewed; 105 AA.
AC Q8XFC1; Q7AN56;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Heat shock protein HspQ {ECO:0000255|HAMAP-Rule:MF_01194};
GN Name=hspQ {ECO:0000255|HAMAP-Rule:MF_01194};
GN OrderedLocusNames=STY1102, t1841;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
CC -!- FUNCTION: Involved in the degradation of certain denaturated proteins,
CC including DnaA, during heat shock stress. {ECO:0000255|HAMAP-
CC Rule:MF_01194}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01194}.
CC -!- SIMILARITY: Belongs to the HspQ family. {ECO:0000255|HAMAP-
CC Rule:MF_01194}.
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DR EMBL; AE014613; AAO69459.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD08205.1; -; Genomic_DNA.
DR RefSeq; NP_455577.1; NC_003198.1.
DR RefSeq; WP_000561983.1; NZ_WSUR01000013.1.
DR AlphaFoldDB; Q8XFC1; -.
DR SMR; Q8XFC1; -.
DR STRING; 220341.16502254; -.
DR EnsemblBacteria; AAO69459; AAO69459; t1841.
DR GeneID; 66755429; -.
DR KEGG; stt:t1841; -.
DR KEGG; sty:STY1102; -.
DR PATRIC; fig|220341.7.peg.1108; -.
DR eggNOG; COG3785; Bacteria.
DR HOGENOM; CLU_123865_1_0_6; -.
DR OMA; LRTAPWY; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.390; -; 1.
DR HAMAP; MF_01194; HspQ; 1.
DR InterPro; IPR011722; Hemimethylated_DNA-bd_dom.
DR InterPro; IPR036623; Hemimethylated_DNA-bd_sf.
DR InterPro; IPR022866; HspQ.
DR Pfam; PF08755; YccV-like; 1.
DR SMART; SM00992; YccV-like; 1.
DR SUPFAM; SSF141255; SSF141255; 1.
DR TIGRFAMs; TIGR02097; yccV; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Stress response.
FT CHAIN 1..105
FT /note="Heat shock protein HspQ"
FT /id="PRO_0000315311"
FT REGION 76..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 105 AA; 11996 MW; B75D569FE9DCB71E CRC64;
MIASKFGIGQ QVRHSLLGYL GVVVDIDPEY SLDEPSPDEL AVNDELRAAP WYHVVMEDDD
GQPVHTYLAE AQLRSEMRDE HPEQPSMDEL ARTIRKQLQA PRLRN