ID   A0A0F2P757_9GAMM        Unreviewed;       290 AA.
AC   A0A0F2P757;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   03-MAY-2023, entry version 29.
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=VR73_03210 {ECO:0000313|EMBL:KJS09250.1};
OS   Gammaproteobacteria bacterium BRH_c0.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS09250.1, ECO:0000313|Proteomes:UP000033581};
RN   [1] {ECO:0000313|EMBL:KJS09250.1, ECO:0000313|Proteomes:UP000033581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS09250.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS09250.1}.
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DR   EMBL; LADM01000024; KJS09250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2P757; -.
DR   STRING; 1629722.VR73_03210; -.
DR   PATRIC; fig|1629722.3.peg.3075; -.
DR   Proteomes; UP000033581; 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; 1.10.287.480; helix hairpin bin; 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   InterPro; IPR023212; Hsp33_helix_hairpin_bin_dom_sf.
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00117}.
FT   DISULFID        231..233
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
FT   DISULFID        264..267
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   290 AA;  32604 MW;  81CB4A8944745DBB CRC64;
     MANKDQLHRF IFDNSDVRGE IISLSDSYLS VLKNSPQSTV IATLLGEMLA AAGLLSATMK
     FDGIITLQAR GDGDLSLLMA DCTRHDSLRG IARVKEGANP QDQDFRQLLG HGHLSITIDP
     AEGERYQGIV PLERDTLGAC LEDYFTMSEQ LPTRLWLFAD GQHAAGLLLQ ALPSQQQSVE
     ERNDYWQHLC ILADTLSRDE MLSLDNITIL TRLFHEENLR LFDPRELRFA CSCSEARTLD
     MLLSLGQEEV LSVVEEMGRV DVECQFCHQQ YSFGRDQVES LFSGQPRTLH
//