(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHM3_GEOS0

ID   A0A0F6BHM3_GEOS0        Unreviewed;       296 AA.
AC   A0A0F6BHM3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=33 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00117};
DE   AltName: Full=Heat shock protein 33 homolog {ECO:0000256|HAMAP-Rule:MF_00117};
DE            Short=HSP33 {ECO:0000256|HAMAP-Rule:MF_00117};
GN   Name=hslO {ECO:0000256|HAMAP-Rule:MF_00117};
GN   OrderedLocusNames=GY4MC1_0068 {ECO:0000313|EMBL:ADP72924.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72924.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72924.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72924.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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:0000256|HAMAP-
CC       Rule:MF_00117, ECO:0000256|SAAS:SAAS01084509}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00117,
CC       ECO:0000256|SAAS:SAAS01084524}.
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:0000256|HAMAP-Rule:MF_00117}.
CC   -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00117, ECO:0000256|SAAS:SAAS01084516}.
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DR   EMBL; CP002293; ADP72924.1; -; Genomic_DNA.
DR   RefSeq; WP_013399817.1; NC_014650.1.
DR   EnsemblBacteria; ADP72924; ADP72924; GY4MC1_0068.
DR   GeneID; 29237310; -.
DR   KEGG; gmc:GY4MC1_0068; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   BioCyc; GSP581103:G1GOQ-81-MONOMER; -.
DR   Proteomes; UP000002034; 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;
DR   PRODOM; A0A0F6BHM3.
DR   SWISS-2DPAGE; A0A0F6BHM3.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084514};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084515};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084518};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084519};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00117, ECO:0000256|SAAS:SAAS01084517}.
FT   DISULFID    237    239       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00117}.
FT   DISULFID    270    273       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00117}.
SQ   SEQUENCE   296 AA;  32075 MW;  D3D812E3CD57E7B2 CRC64;
     MSDYLVKALA YDGQVRAYAA RTTDTVSEAQ RRHQTWPTAS AALGRAITAG VMMGAMLKGD
     DKLTIKIDGG GPIGTILVDS NAKGEVRGYV TNPHVHFDLN EHGKLDVAKA VGTNGMLTVV
     KDLGLRDFFT GQVPIVSGEL GEDFTYYFAS SEQVPSSVGV GVLVNPDNTI LAAGGFIIQL
     MPGTEEKTID EIEKRLRTIP PVSKMVESGL TPEEILEELL GKGNVKVLET IPVAFVCRCS
     RERIADALIS LGAQEIQDII DKEGYAEASC HFCNETYHFS KEELQQLKQL ADAKEE
//

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