ID   HSLO_SYNR3              Reviewed;         302 AA.
AC   A5GTZ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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};
GN   OrderedLocusNames=SynRCC307_1447;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) 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; CT978603; CAK28350.1; -; Genomic_DNA.
DR   RefSeq; WP_011935864.1; NC_009482.1.
DR   AlphaFoldDB; A5GTZ1; -.
DR   SMR; A5GTZ1; -.
DR   STRING; 316278.SynRCC307_1447; -.
DR   EnsemblBacteria; CAK28350; CAK28350; SynRCC307_1447.
DR   KEGG; syr:SynRCC307_1447; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_3; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   Proteomes; UP000001115; 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..302
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000015588"
FT   DISULFID        244..246
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        277..280
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   302 AA;  32323 MW;  8C25E0928C2FF032 CRC64;
     MADRLVRAMA AGGGIRLVAV TTTETTRMAR ERHQLSFLAS ALLGRAMTAG LLLASSMKVA
     HGRVTLRTQS DGLLKGLSVD AGRDGRVRGY VGNPSLELDL VGDPASFDFK QALGTGYLNV
     MRDEGQGPPY SSTVELVSGC IGEDVASYLL HSEQTPSAVF VGEHIDSSGI RCSGGVLVQV
     LPKAAREPAL VALLEDRCRE ITGFSQRLEA CQGDLHSLLR DVFPDLDPEV LADEQAEQPV
     EFFCPCTRER SRGALALLGA EELADMIEKD NGAELTCHFC GEVYRFSGED LAALIEALPR
     SA