ID   HSLO_SALTY              Reviewed;         292 AA.
AC   Q8ZLJ4;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
DT   25-MAY-2022, entry version 108.
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=STM3498;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL22360.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL22360.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_462401.3; NC_003197.2.
DR   AlphaFoldDB; Q8ZLJ4; -.
DR   SMR; Q8ZLJ4; -.
DR   STRING; 99287.STM3498; -.
DR   PaxDb; Q8ZLJ4; -.
DR   EnsemblBacteria; AAL22360; AAL22360; STM3498.
DR   GeneID; 1255021; -.
DR   KEGG; stm:STM3498; -.
DR   PATRIC; fig|99287.12.peg.3697; -.
DR   HOGENOM; CLU_054493_0_0_6; -.
DR   OMA; DMQCECC; -.
DR   PhylomeDB; Q8ZLJ4; -.
DR   Proteomes; UP000001014; 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..292
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000192197"
FT   DISULFID        230..232
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        263..266
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   292 AA;  32369 MW;  7C2BDBC33FA93EC7 CRC64;
     MPQHDQLHRY LFENFAVRGE LVTVSETLQQ ILDNHNYPQP VKTVLAELLV ATSLLTATLK
     FAGDITVQLQ GDGPLSLAVI NGNNQQQMRG VARVQGDIPD NADLKTLVGN GYLVITITPE
     EGERYQGVVG LEGDTLAACL EDYFLRSEQL PTRLFIRTGD VDGKPAAGGM LLQVMPAQNA
     QAEDFDHLAM LTETIKSEEL LTLPANDVLW RLYHEEEVTL YDPQNVEFKC TCSRERCAGA
     LKTLPDEEVD SILAEEGEID MHCDYCGNHY LFNAMDIAEI RNNASPADPQ VH