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HSLO_THESQ
ID   HSLO_THESQ              Reviewed;         290 AA.
AC   B1LBT1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=TRQ2_1435;
OS   Thermotoga sp. (strain RQ2).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC   unclassified Thermotoga.
OX   NCBI_TaxID=126740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RQ2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga sp. RQ2.";
RL   Submitted (MAR-2008) 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; CP000969; ACB09779.1; -; Genomic_DNA.
DR   RefSeq; WP_012311127.1; NC_010483.1.
DR   AlphaFoldDB; B1LBT1; -.
DR   SMR; B1LBT1; -.
DR   EnsemblBacteria; ACB09779; ACB09779; TRQ2_1435.
DR   KEGG; trq:TRQ2_1435; -.
DR   HOGENOM; CLU_054493_1_0_0; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   Proteomes; UP000001687; 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; Zinc.
FT   CHAIN           1..290
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000095039"
FT   DISULFID        231..233
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        263..266
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   290 AA;  32583 MW;  4F603779CDBA4DE2 CRC64;
     MIYYGTMFDH KVRFSIVRMR EVVEEARNRH VLSYLATVVL GRALIGAALV TPWLAEKERW
     TLDIEGSGPI RRVVAQSTSE FTVRGYVANP KVELPLNEKG KFDVAGAIGQ GVLRVVRDLG
     LKTPFVSQVP LVSGEIAEDL AYYFAVSEQI PSAFSIGVLV DSGGVKIAGG FAVQIIDRTL
     EQEKVELIER NIKNLPYITE LFQKAEPLDV LERIFGEKVG FVETAEIRYK CDCNREKAKN
     ALLVLDKKEL EDMRKEGKGE VVCKWCNTKY VFSEEELEEL LKFKVDNSGS
 
 
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