ID   HSLO_SYNE7              Reviewed;         297 AA.
AC   Q31QS8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
GN   OrderedLocusNames=Synpcc7942_0559;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB56591.1; -; Genomic_DNA.
DR   RefSeq; WP_011243275.1; NC_007604.1.
DR   AlphaFoldDB; Q31QS8; -.
DR   SMR; Q31QS8; -.
DR   STRING; 1140.Synpcc7942_0559; -.
DR   PRIDE; Q31QS8; -.
DR   EnsemblBacteria; ABB56591; ABB56591; Synpcc7942_0559.
DR   KEGG; syf:Synpcc7942_0559; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_3; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_0559-MON; -.
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..297
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000238107"
FT   DISULFID        239..241
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        272..275
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   297 AA;  31633 MW;  956195A41DF0EFC5 CRC64;
     MADQLIRATA AGGGIRAVGV ITTDLTAEAQ RKHGLSFVAT TALGRSMAAG LLLASSMKKE
     GSRVNLRIRS AGPLGGLMVD AGLDGTVRGY VEHPAIEIEP NTQGLPDVGR AIGPGYLHVM
     RDVGYGQPYT STVELVNGEI GDDVAYYLAS SEQTPSAILL GVYLDRQGVE AAGGLLIQVL
     PQAARDPELV SLLESRISHL KGFTQLLRSG KDLPEILEDL LGDLDLTILA EPRSLRFFCP
     CTHQRMLGAL KIFGAPELRD MIAKDQGAEA TCEFCSEVYQ ASIEELEELI SDLETAA