(data stored in ACNUC7421 zone)

SWISSPROT: HSLO_PSEHT

ID   HSLO_PSEHT              Reviewed;         281 AA.
AC   Q3ILP2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 73.
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=PSHAa0229;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85332.1; -; Genomic_DNA.
DR   RefSeq; WP_011326946.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILP2; -.
DR   SMR; Q3ILP2; -.
DR   STRING; 326442.PSHAa0229; -.
DR   EnsemblBacteria; CAI85332; CAI85332; PSHAa0229.
DR   KEGG; pha:PSHAa0229; -.
DR   PATRIC; fig|326442.8.peg.220; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261998; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; POG091H01DJ; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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.
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; Q3ILP2.
DR   SWISS-2DPAGE; Q3ILP2.
KW   Chaperone; Complete proteome; Cytoplasm; Disulfide bond;
KW   Redox-active center; Reference proteome; Zinc.
FT   CHAIN         1    281       33 kDa chaperonin.
FT                                /FTId=PRO_0000238082.
FT   DISULFID    229    231       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00117}.
FT   DISULFID    262    265       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00117}.
SQ   SEQUENCE   281 AA;  31760 MW;  1DD5781A4A35AFAE CRC64;
     MQQDLLHRYL FDNLDVRGEL VQIENAYNEM IANHNYPDAV KALLGELLVA TCLLTATLKF
     EGEIAVQLQG DGPVKYAVIN GDDKQNMRGI ARLQSEVTGS TVKELIGQGY MVITITPTKG
     ERYQGIVPLE HETLSECIEA YFEQSEQLKT RLWFATDTTE GNAKACGLFL QVLPVDKQKS
     IEDFAHLEAL SHTIKDEELL ELDANTVLTR LYHEDNPRVF EPQSIQFKCG CTREKTMTAL
     VNIGQQALLD DVAEHGEIKI SCHYCLKDYL FDEQDVKNIF N
//

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