ID   HSLO_PASMU              Reviewed;         288 AA.
AC   Q9CKQ9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=PM1547;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03631.1; -; Genomic_DNA.
DR   RefSeq; WP_005718232.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKQ9; -.
DR   SMR; Q9CKQ9; -.
DR   STRING; 747.DR93_391; -.
DR   EnsemblBacteria; AAK03631; AAK03631; PM1547.
DR   KEGG; pmu:PM1547; -.
DR   HOGENOM; CLU_054493_0_0_6; -.
DR   OMA; DMQCECC; -.
DR   Proteomes; UP000000809; 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; Zinc.
FT   CHAIN           1..288
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000192189"
FT   DISULFID        233..235
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        267..270
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   288 AA;  32140 MW;  879DE20AC52BF936 CRC64;
     MTDNTDNDKL YRYLFQDRAV RGEWVRLNQT FTDTLNTHQY PKVIQNLLGE MMVATSLLTA
     TLKFEGDITV QVQGDGPLKL ALVNGNHQQQ IRALARLQAD VSDDMSLAQL VGKGVLVITI
     APTEGERYQG VIALDKPTIT ACLEDYFVRS EQLQTQLIIR AGEFEGQPVA AGMLLQIMPD
     GSGSPEDFEH LATLAATVKE EELFGLTAEE LLYRLYHEER VEIFPSQPIS FFCGCSQERS
     GAALLLISDE ELDEVLAEHN GTIDMQCECC GTHYFFNKAA IMQLKVEK