HSLO_PROM4
ID HSLO_PROM4 Reviewed; 300 AA.
AC A9BA44;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=P9211_07751;
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=93059;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211;
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; CP000878; ABX08706.1; -; Genomic_DNA.
DR RefSeq; WP_012195328.1; NC_009976.1.
DR AlphaFoldDB; A9BA44; -.
DR SMR; A9BA44; -.
DR STRING; 93059.P9211_07751; -.
DR EnsemblBacteria; ABX08706; ABX08706; P9211_07751.
DR KEGG; pmj:P9211_07751; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_1_0_3; -.
DR OMA; DMQCECC; -.
DR Proteomes; UP000000788; 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..300
FT /note="33 kDa chaperonin"
FT /id="PRO_1000095025"
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 300 AA; 32781 MW; EF1529465126F727 CRC64;
MNDTLVRATA ANGGIRLVAA ITTNALKEAK SRHKLSYLTS ALMGRAMSAS LLLASSMKVL
HGRVTLKIQS DGPIKGLTVD ACRDGSVRGF LGNPSLELDL VKSKEGHHCF DFANATGKGY
LHVIRDIGEG DPYSSTVELV GGGIGEDIAS YLLHSEQTPS AVFVGEKIKH KELVCSGGLI
AQILPKASQD RSLAELLEEN CNTITSFSER LFEYKDNLSG LLKDLFYNLN PEIVKGPSAR
QEIKYRCKCS RDRSISALKL LGNSEIKSIL NEDKKAEITC EFCKNVYQIE EEELRSLVDI