(data stored in SCRATCH zone)

SWISSPROT: C6AZH2_RHILS

ID   C6AZH2_RHILS            Unreviewed;       330 AA.
AC   C6AZH2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   RecName: Full=33 kDa chaperonin {ECO:0000256|SAAS:SAAS00739901};
GN   OrderedLocusNames=Rleg_0187 {ECO:0000313|EMBL:ACS54498.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54498.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54498.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54498.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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.
CC       {ECO:0000256|SAAS:SAAS00739892}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00739897}.
CC   -!- SIMILARITY: Belongs to the HSP33 family.
CC       {ECO:0000256|SAAS:SAAS00739880}.
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DR   EMBL; CP001622; ACS54498.1; -; Genomic_DNA.
DR   RefSeq; WP_012755914.1; NC_012850.1.
DR   ProteinModelPortal; C6AZH2; -.
DR   EnsemblBacteria; ACS54498; ACS54498; Rleg_0187.
DR   KEGG; rlg:Rleg_0187; -.
DR   HOGENOM; HOG000261999; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; POG091H01DJ; -.
DR   BioCyc; RLEG395491:GHX2-189-MONOMER; -.
DR   Proteomes; UP000002256; Chromosome.
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   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; C6AZH2.
DR   SWISS-2DPAGE; C6AZH2.
KW   Chaperone {ECO:0000256|SAAS:SAAS00739870};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00739859};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00739861};
KW   Redox-active center {ECO:0000256|SAAS:SAAS00739906};
KW   Zinc {ECO:0000256|SAAS:SAAS00739879}.
SQ   SEQUENCE   330 AA;  36339 MW;  102E3DE81673EF76 CRC64;
     MAEAAAALGQ FDFAGDDHVV PFQVEGLDVR GRAVQLGPML DAILERHHYP APVARLLAEV
     VVLTVLLGTS LKFDGKFTVQ TKGDGPVDLL VADFSTPENV RAYARFDQAL LNKAIESGET
     EPEQLLGKGV LAFTIDQGKF SQPYQGIVPL DGTTLEDIAG VYFRQSEQIP TRVRLAAAEL
     FDRDDAGKPR HRWRAGGLVA QFLPEAPERM RQPDLHGGDG DTGSRPHGED DAWLEARSLV
     ETIDADELTD PLVGTERLLF RLFHERGVRV YEPRAVFDRC SCSRDKIKGV LKGFSAEEIE
     ASQEDGEIAV TCEFCSTTYR FEPAELQPAE
//

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