ID   HSLO_PSEAE              Reviewed;         297 AA.
AC   Q9HTZ6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=PA5193;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG08578.1; -; Genomic_DNA.
DR   PIR; H82996; H82996.
DR   RefSeq; NP_253880.1; NC_002516.2.
DR   RefSeq; WP_003096245.1; NZ_QZGE01000002.1.
DR   AlphaFoldDB; Q9HTZ6; -.
DR   SMR; Q9HTZ6; -.
DR   STRING; 287.DR97_2562; -.
DR   PaxDb; Q9HTZ6; -.
DR   PRIDE; Q9HTZ6; -.
DR   DNASU; 879313; -.
DR   EnsemblBacteria; AAG08578; AAG08578; PA5193.
DR   GeneID; 879313; -.
DR   KEGG; pae:PA5193; -.
DR   PATRIC; fig|208964.12.peg.5443; -.
DR   PseudoCAP; PA5193; -.
DR   HOGENOM; CLU_054493_0_0_6; -.
DR   InParanoid; Q9HTZ6; -.
DR   OMA; DMQCECC; -.
DR   PhylomeDB; Q9HTZ6; -.
DR   BioCyc; PAER208964:G1FZ6-5312-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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; Zinc.
FT   CHAIN           1..297
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000192193"
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;  32834 MW;  93F63437259356F0 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 SISIDCQFCN QRYLFDASDV AQLFAGAGSQ GPSETRH