HSLO_GEOSE
ID HSLO_GEOSE Reviewed; 296 AA.
AC Q9F984;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 69.
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 Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=V;
RA Vasquez C., Pichuantes S., Saavedra C.;
RL Submitted (OCT-1999) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG28532.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF198621; AAG28532.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q9F984; -.
DR SMR; Q9F984; -.
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..296
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192166"
FT DISULFID 237..239
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 270..273
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ SEQUENCE 296 AA; 32050 MW; 0245C2A34363F0F5 CRC64;
MGDYLVKALA YDGQVRACAA RTTETVGEAP RRHQTWPTAS AALGRALTAG SMMGAMLKGD
ETLTIKIDGG GPIGTILVDS NAKGEVRGYV TNPHVHFELN EHGKLDVARA VGKNGMLTFV
KDLGLRDFFT GQVPIISGEL GEDFTYYFAS SEQVPSSVGV GVLVNPDHTI LAAGGFILQL
MPGTEEKTID QIERRLQTIP PVSRMVESGL TPEEILEELL GKGNVKVLET LPVAFVCRCS
RERIADALIS LGAQEIQDII DKEGYAEASC HFCNETYHFT KEELKQLKQL ADAKKA