ID   HSLO_CAUVN              Reviewed;         302 AA.
AC   B8GYL6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=CCNA_02324;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL95789.1; -; Genomic_DNA.
DR   RefSeq; WP_010920102.1; NC_011916.1.
DR   RefSeq; YP_002517697.1; NC_011916.1.
DR   AlphaFoldDB; B8GYL6; -.
DR   SMR; B8GYL6; -.
DR   PRIDE; B8GYL6; -.
DR   EnsemblBacteria; ACL95789; ACL95789; CCNA_02324.
DR   GeneID; 7332278; -.
DR   KEGG; ccs:CCNA_02324; -.
DR   PATRIC; fig|565050.3.peg.2275; -.
DR   HOGENOM; CLU_054493_0_1_5; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   PhylomeDB; B8GYL6; -.
DR   Proteomes; UP000001364; 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; 1.10.287.480; -; 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   InterPro; IPR023212; Hsp33_helix_hairpin_bin_dom_sf.
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; Stress response; Zinc.
FT   CHAIN           1..302
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000119254"
FT   DISULFID        255..257
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        288..291
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   302 AA;  32670 MW;  D2E49F360A102849 CRC64;
     MTDIAPDTGV LDDVVSAFQI ENLPVRGRVV RLGAAIDEVL TRHDYPEPVA NLLGEACALA
     ALVGSSLKFE GRLIVQAQGD GPVRYVVVDY DTSGGLRGYC RFDPEEVAAV SEGFVRPGAK
     TLLGGGVFIM TLDQGPDMDR YQGVTPIEGE TLALCAEQYF AQSEQTPTRV RLAVGQADTG
     QGATWRAGGI LIQVIAGDQA RGETQDAWTH VQALFETTGE DELIDPTVST PTLLWRLFNE
     DGVRLLDEKP LKAFCRCSED RIGVVMDSFS AEEVAEMVEP DGKIHVTCEY CSRIYKLDPP
     GA