ID A0A1T4LQ87_9FIRM Unreviewed; 294 AA.
AC A0A1T4LQ87;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=33 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00117};
DE AltName: Full=Heat shock protein 33 homolog {ECO:0000256|HAMAP-Rule:MF_00117};
DE Short=HSP33 {ECO:0000256|HAMAP-Rule:MF_00117};
GN Name=hslO {ECO:0000256|HAMAP-Rule:MF_00117};
GN ORFNames=SAMN02745114_00979 {ECO:0000313|EMBL:SJZ56890.1};
OS Eubacterium coprostanoligenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=290054 {ECO:0000313|EMBL:SJZ56890.1, ECO:0000313|Proteomes:UP000190657};
RN [1] {ECO:0000313|EMBL:SJZ56890.1, ECO:0000313|Proteomes:UP000190657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51222 {ECO:0000313|EMBL:SJZ56890.1,
RC ECO:0000313|Proteomes:UP000190657};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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:0000256|HAMAP-Rule:MF_00117}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00117}.
CC -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000256|HAMAP-
CC Rule:MF_00117}.
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DR EMBL; FUWW01000009; SJZ56890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4LQ87; -.
DR STRING; 290054.SAMN02745114_00979; -.
DR OrthoDB; 9776534at2; -.
DR Proteomes; UP000190657; Unassembled WGS sequence.
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; Hsp33 domain; 1.
DR Gene3D; 3.90.1280.10; HSP33 redox switch-like; 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; 33 KDA CHAPERONIN; 1.
DR PANTHER; PTHR30111:SF1; 33 KDA CHAPERONIN; 1.
DR Pfam; PF01430; HSP33; 1.
DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR SUPFAM; SSF64397; Hsp33 domain; 1.
DR SUPFAM; SSF118352; HSP33 redox switch-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00117};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00117};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00117};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_00117}; Reference proteome {ECO:0000313|Proteomes:UP000190657};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00117}.
FT DISULFID 237..239
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
FT DISULFID 270..273
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
SQ SEQUENCE 294 AA; 31756 MW; A67A2DAF6AE98E67 CRC64;
MGKIVRYIAV DGSAFVIATD STDIVYEAEQ IHKTSATVTA ALGRLITATS MMGDMLKDKE
DSITVRMNGA GPCGDLIAVS DYEGNTRGYV QNPVVEIPLK ENGKLDVSGA VGTDGQLYVI
KDIGMKEPYV GQVPIVSGEI AEDITNYFAT SEQTPSVCAL GVLVNPDLTV KKAGGYIIQL
LPGCPDDIID IIEKNVSEIP SVTTMLDEGM IPDEIAIKAM QGIELDKLDE STAEYRCNCS
RKKVENALIS TGIEALTEMA NDDKDTKVEC HFCNKEYVFT PQDIKQIINA STKK
//
