ID   HSLO_STRSV              Reviewed;         290 AA.
AC   A3CQV0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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}; OrderedLocusNames=SSA_2190;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN45555.1; -; Genomic_DNA.
DR   RefSeq; YP_001036105.1; NC_009009.1.
DR   AlphaFoldDB; A3CQV0; -.
DR   SMR; A3CQV0; -.
DR   STRING; 388919.SSA_2190; -.
DR   EnsemblBacteria; ABN45555; ABN45555; SSA_2190.
DR   KEGG; ssa:SSA_2190; -.
DR   PATRIC; fig|388919.9.peg.2075; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_9; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   Proteomes; UP000002148; 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..290
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000015584"
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;  31773 MW;  EF4DE3F2FD41690A CRC64;
     MDKIIKTISE NGSFRAYVLD STETVRTAQE KHQTQASSTV ALGRTLIASQ ILAANEKGQT
     KITVKVLGTS SLGAIITVAD TEGNVKGYVQ NPGVDIKKTA TGEVLVGPFV GQGEFLVITD
     YGTGNPYNSM TPLISGEIGE DLAFYLTESQ QTPSAVGLNV LLDENDKVKV AGGFLVQVLP
     GAKEAEIARF EKRIQEMPAI SRLLESDDHI EALLAAIYGN EPYKRLSEEE IRFQCDCNKE
     RFMNALATLP KADLEEMRDQ DQGAEIVCQF CQTAYHFDQN DLEELIRDKS