ID A0A1U7NXE0_9DEIO Unreviewed; 303 AA.
AC A0A1U7NXE0;
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=BOO71_0008305 {ECO:0000313|EMBL:OLV17595.1};
OS Deinococcus marmoris.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=249408 {ECO:0000313|EMBL:OLV17595.1, ECO:0000313|Proteomes:UP000186607};
RN [1] {ECO:0000313|EMBL:OLV17595.1, ECO:0000313|Proteomes:UP000186607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOPRI26562 {ECO:0000313|EMBL:OLV17595.1,
RC ECO:0000313|Proteomes:UP000186607};
RA Kim J.H., Oh H.-M.;
RT "Genome Analysis of Deinococcus marmoris KOPRI26562.";
RL Submitted (JAN-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLV17595.1}.
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DR EMBL; MSTI01000093; OLV17595.1; -; Genomic_DNA.
DR RefSeq; WP_075833481.1; NZ_MSTI01000093.1.
DR AlphaFoldDB; A0A1U7NXE0; -.
DR STRING; 249408.BOO71_0008305; -.
DR eggNOG; COG1281; Bacteria.
DR OrthoDB; 9776534at2; -.
DR Proteomes; UP000186607; 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}; Stress response {ECO:0000313|EMBL:OLV17595.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00117}.
FT DISULFID 245..247
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
FT DISULFID 277..280
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
SQ SEQUENCE 303 AA; 31906 MW; 47C2288C5AA2402C CRC64;
MTASSISDSF LLRGTAAGNT LRLVGMESTR IVEDARLRHH LSKTATAALG RTLTASALLA
VVLGKRGDSR VTVRVEGGGP VGWIVAEGSA DGQIRGYVRQ PDADLPLRES DGKLDVSGIV
GSTGELAVTR LLDNGEPYTG SIELVSGEIA EDISSYLGVS EQIPNAVLLG VYEEGGRVAH
AGGLLVQAMP GVSDETLAHL EANIRALGQI TDGLRRGGIL DVMNRVTEGL GLTLAPGAQA
ARFGCRCSRQ KAEDSLKFFN AEERQDMMDT GGQEVVCHWC GEKYHITPGE IAALDATVER
ARA
//
