ID   HSLO_SYNP2              Reviewed;         298 AA.
AC   B1XJZ5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, 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};
GN   OrderedLocusNames=SYNPCC7002_A1123;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-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; CP000951; ACA99123.1; -; Genomic_DNA.
DR   RefSeq; WP_012306746.1; NC_010475.1.
DR   AlphaFoldDB; B1XJZ5; -.
DR   SMR; B1XJZ5; -.
DR   STRING; 32049.SYNPCC7002_A1123; -.
DR   EnsemblBacteria; ACA99123; ACA99123; SYNPCC7002_A1123.
DR   KEGG; syp:SYNPCC7002_A1123; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_3; -.
DR   OMA; DMQCECC; -.
DR   Proteomes; UP000001688; 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; Stress response; Zinc.
FT   CHAIN           1..298
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000095036"
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   298 AA;  31764 MW;  1EFF89CE7B566CAC CRC64;
     MADQLIRGTA ADNGIRVVGV ISTNLTEEAR QRHKLSYVAT AALGRTMASA LLISSSMKKQ
     EARLNLRIKG DGPLGGLLVD AGPDGTVRGY VQNPGVELPP NAKGKLDVGG AVGKGFLYAV
     KDFGRGYPYS STVELVSGEI GDDVTHYLAT SEQTPSALLV GVFVGAEGVT AAGGILLQIL
     PKAARDESLV AKLESRLGQL SGFTPLLQQG KSLHDIFQDL LGDEDLNIFP ETQMVRFDCG
     CTFERMMGAL KMLGQDELLD MIEKDGGAEA TCNFCNEVYH ADVDHLSRLV EELKADAH