ID   HSLO_GLOVI              Reviewed;         306 AA.
AC   Q7NIA2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; Synonyms=hsp33;
GN   OrderedLocusNames=glr2281;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC90222.1; -; Genomic_DNA.
DR   RefSeq; NP_925227.1; NC_005125.1.
DR   RefSeq; WP_011142278.1; NC_005125.1.
DR   AlphaFoldDB; Q7NIA2; -.
DR   SMR; Q7NIA2; -.
DR   STRING; 251221.35212849; -.
DR   EnsemblBacteria; BAC90222; BAC90222; BAC90222.
DR   KEGG; gvi:glr2281; -.
DR   PATRIC; fig|251221.4.peg.2316; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_3; -.
DR   InParanoid; Q7NIA2; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   PhylomeDB; Q7NIA2; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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..306
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000192178"
FT   DISULFID        242..244
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        275..278
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   306 AA;  32668 MW;  40E3396B4EB1577A CRC64;
     MADQLVRATA AQGRIRAVGV LSTRLTEEAR GRHKLSYVAT AALGRTMAAG LLIASNFKQT
     EARVNLRLQG DGPLGGILVD AGADGTVRGY VKNPQVELPP SPKGKLDVGR AVGANGFLYV
     VKDLGYGYPF SGTTELVSGE IGDDVTHYLV TSEQVASALM LGVFVGADGV DAAGGLLLQV
     MPSADGQEDE ELAATLERRL ASVEGFTPLV RSGKRIPQIL EELLGDMGLE IFPEVQLVRF
     HCHCSPQRVL GALKMMGEAE LLDMIEKDGG AEATCHFCNQ VYQVKASELE TLVEQLRSER
     EVSSQE