ID   HSLO_STRP9              Reviewed;         290 AA.
AC   P0C0C4; Q9ZB45;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
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};
OS   Streptococcus pyogenes serotype M49.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301452;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CS101 / Serotype M49;
RX   PubMed=10096074; DOI=10.1046/j.1365-2958.1999.01241.x;
RA   Podbielski A., Woischnik M., Leonard B.A.B., Schmidt K.H.;
RT   "Characterization of nra, a global negative regulator gene in group A
RT   streptococci.";
RL   Mol. Microbiol. 31:1051-1064(1999).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC97154.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U49397; AAC97154.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; P0C0C4; -.
DR   SMR; P0C0C4; -.
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_0000192216"
FT   DISULFID        235..237
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        268..271
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   290 AA;  31582 MW;  E55E7B6A773184B9 CRC64;
     MDKIIKSIAQ SGAFRAYVLD STETVALAQE KHNTLSSSTV ALGRTLIANQ ILAANQKGDS
     KITVKVIGDS SFGHIISVAD TKGHVKGYIQ NTGVDIKKTE TGEVLVGPFM GNGHFVTIID
     YGTGNPYTST TPLITGEIGE DFAYYLTESE QTPSAIGLNV LLDENDKVKV AGGFMVQVLP
     EASEEEIARY EKRLQEMPAI SHLLASKNHV DALLEAIYGD EPYKRLSEEP LSFQCDCSRE
     RFEAALMTLP KADLQAMIDE DKGAEIVCQF CGTKYQFNES DLEAIISDKA