HSLO_CLOPE
ID HSLO_CLOPE Reviewed; 319 AA.
AC Q8XJ60;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=CPE1901;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81607.1; -; Genomic_DNA.
DR RefSeq; WP_003454848.1; NC_003366.1.
DR AlphaFoldDB; Q8XJ60; -.
DR SMR; Q8XJ60; -.
DR STRING; 195102.gene:10491170; -.
DR EnsemblBacteria; BAB81607; BAB81607; BAB81607.
DR GeneID; 29570737; -.
DR KEGG; cpe:CPE1901; -.
DR HOGENOM; CLU_054493_1_0_9; -.
DR OMA; DMQCECC; -.
DR Proteomes; UP000000818; 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..319
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192171"
FT REGION 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 319 AA; 35063 MW; DEB65CC04EB47F6D CRC64;
MSDKLIRAIA KDGMIRIFAT ETTELVDEAS KIHDCTPTAA AALGRMLTAG TMMGAMLKSD
KEVVTLQING GGMAKGVTVT AYSDCSVKGY IGNPHVDLPL NTENGKLNVG EAIGKNGGLT
VIKDLGLKDP YVGQVPIYSG EIAEDLAYYF TASEQIPSAV ALGVLVDRDH SIKKAGGFII
QLLPGADELL GDLLTYRLDE IPSLTTMLSE GKTIEEVIEF IFDGMDLKIL EEETPKYKCD
CSREKVERAL LSIGYKDLKE LYDEGKEEEL KCHFCNKAYK FTKEDIGKLL EEKEKSIADE
VSEEMKKAEE KEKEEKNKK
