ID   HSLO_THET8              Reviewed;         341 AA.
AC   Q5SJV8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=33 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00117};
DE   AltName: Full=Heat shock protein 33 homolog {ECO:0000255|HAMAP-Rule:MF_00117};
DE            Short=HSP33 {ECO:0000255|HAMAP-Rule:MF_00117};
GN   Name=hslO {ECO:0000255|HAMAP-Rule:MF_00117}; OrderedLocusNames=TTHA0894;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Redox regulated molecular chaperone. Protects both thermally
CC       unfolding and oxidatively damaged proteins from irreversible
CC       aggregation. Plays an important role in the bacterial defense system
CC       toward oxidative stress. {ECO:0000255|HAMAP-Rule:MF_00117}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00117}.
CC   -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC       involving the reactive cysteines. Under reducing conditions zinc is
CC       bound to the reactive cysteines and the protein is inactive.
CC       {ECO:0000255|HAMAP-Rule:MF_00117}.
CC   -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00117}.
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DR   EMBL; AP008226; BAD70717.1; -; Genomic_DNA.
DR   RefSeq; WP_011228278.1; NC_006461.1.
DR   RefSeq; YP_144160.1; NC_006461.1.
DR   AlphaFoldDB; Q5SJV8; -.
DR   SMR; Q5SJV8; -.
DR   STRING; 300852.55772276; -.
DR   EnsemblBacteria; BAD70717; BAD70717; BAD70717.
DR   GeneID; 3169889; -.
DR   KEGG; ttj:TTHA0894; -.
DR   PATRIC; fig|300852.9.peg.886; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_0; -.
DR   OMA; DMQCECC; -.
DR   PhylomeDB; Q5SJV8; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00498; Hsp33; 1.
DR   Gene3D; 3.55.30.10; -; 1.
DR   Gene3D; 3.90.1280.10; -; 1.
DR   HAMAP; MF_00117; HslO; 1.
DR   InterPro; IPR000397; Heat_shock_Hsp33.
DR   InterPro; IPR016154; Heat_shock_Hsp33_C.
DR   InterPro; IPR016153; Heat_shock_Hsp33_N.
DR   PANTHER; PTHR30111; PTHR30111; 1.
DR   Pfam; PF01430; HSP33; 1.
DR   PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR   SUPFAM; SSF118352; SSF118352; 1.
DR   SUPFAM; SSF64397; SSF64397; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Disulfide bond; Redox-active center;
KW   Reference proteome; Zinc.
FT   CHAIN           1..341
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000238109"
FT   DISULFID        245..247
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        278..281
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   341 AA;  36911 MW;  7C50DC5FAC004E51 CRC64;
     MGRILRGLAG EGDLRVVAAE TTDVVEEARL RHGLSPTATA ALGRAMTGAL LLAQLLLKTP
     KERITLRVEG TGPLGGLVVE ADAFGHVRGY VKNPRAEVPL REDGKLNVGE LVGAGALRVD
     RSLPSGEVYT STVPLVSGEI AEDLAHYLWQ SEQIPSAVLL GVRVKGEGEV EVAGGVAVQV
     MPGAREEVLD RLEANLKDLP GLTPLLRERG LEGALEALLA GLGFERTDLR ALGYFQNEIP
     ARFRCRCNRE KALEALVFFT PEEREDMIVK DGGAEVVCHW CGEVYRFSPE EVRSLVAEVR
     CPDCGTLWLY PKGDGTLARI EGETCRCGRK VELPSETRPQ A