ID   HSLO_PROMT              Reviewed;         299 AA.
AC   Q46LN9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=PMN2A_0097;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ57589.1; -; Genomic_DNA.
DR   RefSeq; WP_011293631.1; NC_007335.2.
DR   AlphaFoldDB; Q46LN9; -.
DR   SMR; Q46LN9; -.
DR   STRING; 59920.PMN2A_0097; -.
DR   EnsemblBacteria; AAZ57589; AAZ57589; PMN2A_0097.
DR   KEGG; pmn:PMN2A_0097; -.
DR   HOGENOM; CLU_054493_1_0_3; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   PhylomeDB; Q46LN9; -.
DR   Proteomes; UP000002535; 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; 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   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..299
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000238081"
FT   DISULFID        247..249
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        280..283
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   299 AA;  32672 MW;  9A5E5DA285931F53 CRC64;
     MTDSLVRATA AKGGIRLVAV STTESTKEAK ERHSLSYLTS AIVGRAMSAS LLLASSMKVN
     HGRVTLRISS NGPLKGLTID AGRDGSVRGY VGDPSLELDL IKNKSNHYTF DFKKATGIGY
     LHVIRDDGKG EPHNSTVELI NGGIGEDIAS YLLHSEQTPS AVFVGEKINQ DGIVCSGGLL
     AQILPKAERD YSLIDLLEDR CKEINSFSEL LNKKGNNLIS LIEEIFPDLD QSPSDIISTS
     QEVHFKCRCS RERSLSALKI LGKDELQKMI KEDGKAELTC QFCKNVYLVK EDELISLID