HSPQ_ECOLI
ID HSPQ_ECOLI Reviewed; 105 AA.
AC P0AB20; P75875;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Heat shock protein HspQ;
GN Name=hspQ; Synonyms=yccV; OrderedLocusNames=b0966, JW5970;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 1-6, CHARACTERIZATION, AND INDUCTION.
RX PubMed=15569148; DOI=10.1111/j.1365-2443.2004.00800.x;
RA Shimuta T.R., Nakano K., Yamaguchi Y., Ozaki S., Fujimitsu K.,
RA Matsunaga C., Noguchi K., Emoto A., Katayama T.;
RT "Novel heat shock protein HspQ stimulates the degradation of mutant DnaA
RT protein in Escherichia coli.";
RL Genes Cells 9:1151-1166(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RA Shioi S., Maenaka K., Kohda D., Katayama T., Ueda T.;
RT "Crystal structure of hypothetical protein from Escherichia coli.";
RL Submitted (MAR-2004) to the PDB data bank.
CC -!- FUNCTION: Involved in the degradation of certain denaturated proteins,
CC including DnaA, during heat shock stress.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By heat shock. Transcribed by the sigma-32 subunit of RNA
CC polymerase. {ECO:0000269|PubMed:15569148}.
CC -!- SIMILARITY: Belongs to the HspQ family. {ECO:0000305}.
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DR EMBL; U00096; AAC74052.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35731.1; -; Genomic_DNA.
DR PIR; E64837; E64837.
DR RefSeq; NP_415486.4; NC_000913.3.
DR RefSeq; WP_001295356.1; NZ_STEB01000006.1.
DR PDB; 5YCQ; X-ray; 2.50 A; A=1-105.
DR PDBsum; 5YCQ; -.
DR AlphaFoldDB; P0AB20; -.
DR SMR; P0AB20; -.
DR BioGRID; 4262986; 8.
DR DIP; DIP-48155N; -.
DR STRING; 511145.b0966; -.
DR jPOST; P0AB20; -.
DR PaxDb; P0AB20; -.
DR PRIDE; P0AB20; -.
DR EnsemblBacteria; AAC74052; AAC74052; b0966.
DR EnsemblBacteria; BAA35731; BAA35731; BAA35731.
DR GeneID; 67414146; -.
DR GeneID; 945578; -.
DR KEGG; ecj:JW5970; -.
DR KEGG; eco:b0966; -.
DR PATRIC; fig|1411691.4.peg.1307; -.
DR EchoBASE; EB3488; -.
DR eggNOG; COG3785; Bacteria.
DR InParanoid; P0AB20; -.
DR OMA; LRTAPWY; -.
DR PhylomeDB; P0AB20; -.
DR BioCyc; EcoCyc:G6500-MON; -.
DR EvolutionaryTrace; P0AB20; -.
DR PRO; PR:P0AB20; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0070207; P:protein homotrimerization; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Stress response.
FT CHAIN 1..105
FT /note="Heat shock protein HspQ"
FT /id="PRO_0000168795"
FT REGION 75..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:5YCQ"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:5YCQ"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:5YCQ"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5YCQ"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:5YCQ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5YCQ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5YCQ"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:5YCQ"
SQ SEQUENCE 105 AA; 11779 MW; B0F4FD95DCDF67AA CRC64;
MIASKFGIGQ QVRHSLLGYL GVVVDIDPVY SLSEPSPDEL AVNDELRAAP WYHVVMEDDN
GLPVHTYLAE AQLSSELQDE HPEQPSMDEL AQTIRKQLQA PRLRN
