ID   HSLO_PSEAB              Reviewed;         297 AA.
AC   Q02EH1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=PA14_68610;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ14577.1; -; Genomic_DNA.
DR   RefSeq; WP_003109983.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02EH1; -.
DR   SMR; Q02EH1; -.
DR   PRIDE; Q02EH1; -.
DR   EnsemblBacteria; ABJ14577; ABJ14577; PA14_68610.
DR   KEGG; pau:PA14_68610; -.
DR   HOGENOM; CLU_054493_0_0_6; -.
DR   OMA; DMQCECC; -.
DR   BioCyc; PAER208963:G1G74-5782-MON; -.
DR   Proteomes; UP000000653; 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; Zinc.
FT   CHAIN           1..297
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000015560"
FT   DISULFID        232..234
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        266..269
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   297 AA;  32848 MW;  93F63066608356F0 CRC64;
     MSHSDQSQRF LFDDTDVRGE MVDLERSYSE VLAKHPYPEP VAQLLGEMLA AASLLCGTLK
     FDGLLVLQAR SSGAVPLLMV ECSSDRQVRG LARYSAESIG ADAGMQELMP EGVLTLTVDP
     VKGQRYQGIV ALEGVNLAEC LSNYFASSEQ LPTRFWLNAN GRRARGLLLQ QLPADRLKDP
     EAREASWQHL TTLADTLTAE ELLALDNETV LHRLYHEETV RLFEPQPLVF HCSCSRERSA
     NALVSLGQAD CERLLEEEEG SITIDCQFCN QRYLFDASDV AQLFAGAGSQ GPSETRH