ID   HSLO_ALIFM              Reviewed;         291 AA.
AC   B5FCE6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=VFMJ11_2600;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) 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: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; CP001139; ACH67386.1; -; Genomic_DNA.
DR   RefSeq; WP_005421430.1; NC_011184.1.
DR   AlphaFoldDB; B5FCE6; -.
DR   SMR; B5FCE6; -.
DR   EnsemblBacteria; ACH67386; ACH67386; VFMJ11_2600.
DR   GeneID; 64243163; -.
DR   KEGG; vfm:VFMJ11_2600; -.
DR   HOGENOM; CLU_054493_0_0_6; -.
DR   OMA; DMQCECC; -.
DR   Proteomes; UP000001857; Chromosome I.
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..291
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000095041"
FT   DISULFID        229..231
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        262..265
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   291 AA;  32483 MW;  1F2E06AE2CE12F29 CRC64;
     MANNTLHRYL FEDLSVRGEL VQLDDAYQQI ISSKEYPKPV QNLLGELLVA TTLLTATLKF
     EGSITLQLQG DGPVSLAVIN GDNNQKVRGV ARFEGDIAED ATLHQLMGRG YLVITITPKD
     GERYQGVVAL EGENLAQCFE GYFERSEQLK TRLWLRLGEY EGKPHAAGML LQVMPDGTGS
     ENDFEHLEQL TDTIKNEELF GLPAEDVLYR LYNQDKVQLF EPQDVEFFCG CSRERSGGAI
     VTIDRAEVDD IIKTEGKISL HCDYCGTSYD FDSIDVANLF EQATSGNDTV H