(data stored in ACNUC7421 zone)

SWISSPROT: HSLO_PSEPF

ID   HSLO_PSEPF              Reviewed;         300 AA.
AC   Q3KJP5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
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};
GN   OrderedLocusNames=Pfl01_0267;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Redox regulated molecular chaperone. Protects both
CC       thermally unfolding and oxidatively damaged proteins from
CC       irreversible aggregation. Plays an important role in the bacterial
CC       defense system toward oxidative stress. {ECO:0000255|HAMAP-
CC       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
CC       is 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}.
DR   EMBL; CP000094; ABA72011.1; -; Genomic_DNA.
DR   RefSeq; WP_011331968.1; NC_007492.2.
DR   SMR; Q3KJP5; -.
DR   STRING; 205922.Pfl01_0267; -.
DR   PRIDE; Q3KJP5; -.
DR   EnsemblBacteria; ABA72011; ABA72011; Pfl01_0267.
DR   KEGG; pfo:Pfl01_0267; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261998; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   BioCyc; PFLU205922:G1G4S-268-MONOMER; -.
DR   Proteomes; UP000002704; 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; 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;
DR   PRODOM; Q3KJP5.
DR   SWISS-2DPAGE; Q3KJP5.
KW   Chaperone; Complete proteome; Cytoplasm; Disulfide bond;
KW   Redox-active center; Zinc.
FT   CHAIN         1    300       33 kDa chaperonin.
FT                                /FTId=PRO_0000238084.
FT   DISULFID    235    237       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00117}.
FT   DISULFID    269    272       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00117}.
SQ   SEQUENCE   300 AA;  33324 MW;  43579FC4C5CDD5AF CRC64;
     MTDFLDTDYT QRFIFDDSDT RGELVSLERS YAEVLAKHPY PEPVAQLLGE LMAAASLLVG
     TLKFDGLLIL QARSEGPIPL LMIECSSERE IRGLARYHAE QIPADATLGD LMPNGVLALT
     VDPIAGQRYQ GIVDLDGETL SDCFTNYFVM SQQVGTRFKL CADGRRARGL LLQQLPADRL
     KDEEERAASW QHITALGNTL TADELLSLDN ETVLHRLYHE EQVRLFDVQK LRFHCSCSRE
     RSGNALVSLG LEDAQALVAE QGGQVEIDCQ FCNQRYLFDA ADIAQLFAGA GVETPSDTRH
//

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