HSLO_PROMA
ID HSLO_PROMA Reviewed; 301 AA.
AC Q7VBR5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=Pro_1027;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00072.1; -; Genomic_DNA.
DR RefSeq; NP_875419.1; NC_005042.1.
DR RefSeq; WP_011125179.1; NC_005042.1.
DR AlphaFoldDB; Q7VBR5; -.
DR SMR; Q7VBR5; -.
DR STRING; 167539.Pro_1027; -.
DR PRIDE; Q7VBR5; -.
DR EnsemblBacteria; AAQ00072; AAQ00072; Pro_1027.
DR GeneID; 54200370; -.
DR KEGG; pma:Pro_1027; -.
DR PATRIC; fig|167539.5.peg.1078; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_1_0_3; -.
DR OMA; DMQCECC; -.
DR OrthoDB; 1406579at2; -.
DR Proteomes; UP000001420; 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..301
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192191"
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 301 AA; 32991 MW; 21EA680CAD02B7CF CRC64;
MADSLVRATA ANGSIALVAV LTTESTKEAR RRHSLSYLTT IMLSRAMSAG LLLASSMKVK
QGRVTIKIQS DGPLQGLNVD AGRDGTVRGY VGNPSLELDL IKTSQGNHYF DFKKATGKGY
LHVTRDIGKG EPFTSTVEIE GGGIGEDIAS YLLHSEQVQS AVFVGEIIED QEFICSGALI
AQILPSAVEN KTLINLLDEE CKKITGFSQH LLASKDNLPS LFSHLFPNLN PKIIKTMDNN
QSISFKCRCS RDRSISALKL LGKEELIEIM NEDKKSELTC NFCNEIYNVN EQELKTIIGE
F