HSLO_PROMS
ID HSLO_PROMS Reviewed; 302 AA.
AC A2BQE5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=A9601_07201;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
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; CP000551; ABM70006.1; -; Genomic_DNA.
DR RefSeq; WP_011818168.1; NC_008816.1.
DR AlphaFoldDB; A2BQE5; -.
DR SMR; A2BQE5; -.
DR STRING; 146891.A9601_07201; -.
DR EnsemblBacteria; ABM70006; ABM70006; A9601_07201.
DR KEGG; pmb:A9601_07201; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_1_0_3; -.
DR OMA; DMQCECC; -.
DR OrthoDB; 1406579at2; -.
DR Proteomes; UP000002590; 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; Zinc.
FT CHAIN 1..302
FT /note="33 kDa chaperonin"
FT /id="PRO_1000015557"
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 302 AA; 33568 MW; 63F0B449467094BB CRC64;
MQDRIVRATA ANGGIRLVAV LTTESSLEAK KRHGLSYLTT CILGRAFSAS LLLASSMKIM
HGRVTLRVRS DGPLKGLLVD AGRDGKVRGY VGNPNLELDL VKIDNDKYSF DFTKALGTGY
LNVIRDSGFG EPFTSTVELV NGNIAEDLAS YLYHSEQTPS AVFIGEKIQN KSVICSGGLL
AQVLPKKDTD PLLISLLEER CKEINSFSED LFKSKHNLLE LIRNIFPDID DKSISEKARS
QEVSFKCKCS KQRSLNAMKM LDKSELEDIL KKDGKAELVC EFCKNKYLIN FEEIKSMIEN
QS