(data stored in ACNUC7421 zone)

SWISSPROT: D6XV61_BACIE

ID   D6XV61_BACIE            Unreviewed;       298 AA.
AC   D6XV61;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=Bsel_0068 {ECO:0000313|EMBL:ADH97619.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97619.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97619.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
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., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-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: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; CP001791; ADH97619.1; -; Genomic_DNA.
DR   RefSeq; WP_013171049.1; NC_014219.1.
DR   STRING; 439292.Bsel_0068; -.
DR   EnsemblBacteria; ADH97619; ADH97619; Bsel_0068.
DR   KEGG; bse:Bsel_0068; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261703; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   BioCyc; BSEL439292:G1GLR-75-MONOMER; -.
DR   Proteomes; UP000000271; 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; D6XV61.
DR   SWISS-2DPAGE; D6XV61.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084514};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
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   Reference proteome {ECO:0000313|Proteomes:UP000000271};
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   298 AA;  32507 MW;  FE0795968C4AA911 CRC64;
     MTNDYLVKAL AYEDQVRIYA INSTDMTDEA ARRHQTWRTV TAALGRALSA GTMMGSMLKG
     DEKLTIKIEG NGPASPMVID ANAKGKARGY VGRVDVDPER REDGKLNVGA VVGNEGHISV
     VKDLGMKDYF TGSVPLVSGE LGDDFTYYFA SSEQTPSSVA LGVLIGEEEK VLASGGFILQ
     LMPEASDATI DEVERILQGL PSVTEMLSEG MTPEDIVARL SGGTHRILEK LDTAFECNCS
     RERIETALYS IQEDELELMI TEDEGAETSC HFCNEIYTFT KADLETILSN RKNGIQPE
//

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