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Database: UniProt/SWISS-PROT
Entry: HSLO_GEOSW
LinkDB: HSLO_GEOSW
Original site: HSLO_GEOSW 
ID   HSLO_GEOSW              Reviewed;         295 AA.
AC   C5D392;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
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=GWCH70_0066;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001638; ACS23008.1; -; Genomic_DNA.
DR   RefSeq; WP_012748843.1; NC_012793.1.
DR   SMR; C5D392; -.
DR   STRING; 471223.GWCH70_0066; -.
DR   EnsemblBacteria; ACS23008; ACS23008; GWCH70_0066.
DR   KEGG; gwc:GWCH70_0066; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261703; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   Proteomes; UP000002386; 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; Complete proteome; Cytoplasm; Disulfide bond;
KW   Redox-active center; Reference proteome; Zinc.
FT   CHAIN         1    295       33 kDa chaperonin.
FT                                /FTId=PRO_1000202998.
FT   DISULFID    237    239       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00117}.
FT   DISULFID    270    273       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00117}.
SQ   SEQUENCE   295 AA;  32061 MW;  AB5F85F8B6AE0184 CRC64;
     MSDYLVKALA YDGQVRAYAA RTTDTVSEAQ RRHQTWPTAS AALGRAITAG VMMGAMLKGD
     DKLTIKIDGG GPIGTILVDS NAKGEVRGYV TNPHVHFDLN EHGKLDVAKA VGKNGMLTVV
     KDLGLRDFFT GQVPIISGEL GEDFTYYFAS SEQVPSSVGV GVLVNPDNTI LAAGGFIIQL
     MPGTEEKTIE QIEQRLQTIP PVSKMVESGL TPEEILEELL GKGNVKVLET LPVSFVCRCS
     RERIADAIIS LGPQEIQDIM EKEGYAEASC HFCNETYHFT KEELEQLKQL AEAKN
//
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