ID   HSPQ_SHIFL              Reviewed;         105 AA.
AC   P0AB23; P75875;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Heat shock protein HspQ {ECO:0000255|HAMAP-Rule:MF_01194};
GN   Name=hspQ {ECO:0000255|HAMAP-Rule:MF_01194};
GN   OrderedLocusNames=SF0968, S1034;
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: 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN42596.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP16482.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN42596.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP16482.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_706889.1; NC_004337.2.
DR   RefSeq; WP_001295356.1; NZ_WPGW01000043.1.
DR   AlphaFoldDB; P0AB23; -.
DR   SMR; P0AB23; -.
DR   STRING; 198214.SF0968; -.
DR   EnsemblBacteria; AAN42596; AAN42596; SF0968.
DR   EnsemblBacteria; AAP16482; AAP16482; S1034.
DR   GeneID; 1023941; -.
DR   GeneID; 67414146; -.
DR   KEGG; sfl:SF0968; -.
DR   KEGG; sfx:S1034; -.
DR   PATRIC; fig|198214.7.peg.1127; -.
DR   HOGENOM; CLU_123865_1_0_6; -.
DR   OrthoDB; 1761005at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome; Stress response.
FT   CHAIN           1..105
FT                   /note="Heat shock protein HspQ"
FT                   /id="PRO_0000168798"
FT   REGION          75..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   105 AA;  11779 MW;  B0F4FD95DCDF67AA CRC64;
     MIASKFGIGQ QVRHSLLGYL GVVVDIDPVY SLSEPSPDEL AVNDELRAAP WYHVVMEDDN
     GLPVHTYLAE AQLSSELQDE HPEQPSMDEL AQTIRKQLQA PRLRN