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CH602_BRADU
ID   CH602_BRADU             Reviewed;         550 AA.
AC   P35861;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=blr6979;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110spc4;
RX   PubMed=8101485; DOI=10.1002/j.1460-2075.1993.tb05952.x;
RA   Fischer H.-M., Babst M., Kaspar T., Acuna G., Arigoni F., Hennecke H.;
RT   "One member of a gro-ESL-like chaperonin multigene family in Bradyrhizobium
RT   japonicum is co-regulated with symbiotic nitrogen fixation genes.";
RL   EMBO J. 12:2901-2912(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC       role in assisting protein folding. The GroEL-GroES system forms a nano-
CC       cage that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC         unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00600};
CC   -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC       rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- INDUCTION: Not induced by heat shock.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR   EMBL; Z22604; CAA80318.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC52244.1; -; Genomic_DNA.
DR   PIR; S35309; S35309.
DR   RefSeq; NP_773619.1; NC_004463.1.
DR   RefSeq; WP_011089717.1; NZ_CP011360.1.
DR   AlphaFoldDB; P35861; -.
DR   SMR; P35861; -.
DR   STRING; 224911.27355260; -.
DR   EnsemblBacteria; BAC52244; BAC52244; BAC52244.
DR   GeneID; 64026733; -.
DR   KEGG; bja:blr6979; -.
DR   PATRIC; fig|224911.44.peg.7013; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_5; -.
DR   InParanoid; P35861; -.
DR   OMA; YAFGFDA; -.
DR   PhylomeDB; P35861; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   HAMAP; MF_00600; CH60; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Cpn60/GroEL.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..550
FT                   /note="Chaperonin GroEL 2"
FT                   /id="PRO_0000063295"
FT   BINDING         30..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         87..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         496
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   550 AA;  58273 MW;  4C1DAA55FA499818 CRC64;
     MSAKEVKFGV DARDRMLRGV DILHNAVKVT LGPKGRNVVL DKSFGAPRIT KDGVTVAKEI
     ELEDKFENMG AQMVREVASK SADAAGDGTT TATVLAAAIV REGAKSVAAG MNPMDLKRGI
     DMAVEAVVAD LVKNSKKVTS NEEIAQVGTI SANGDAEIGK FISDAMKKVG NEGVITVEEA
     KSLETELEVV EGMQFDRGYI SPYFVTNADK MRVEMDDAYV LINEKKLSQL NELLPLLEAV
     VQSGKPLVII AEDVEGEALA TLVVNRLRGG LKVAAVKAPG FGDRRKAMLQ DIAILTGGQA
     ISEDLGIKLE NVTLNMLGRA KKVMIDKENT TIVSGAGKKA DIEARVAQIK AQIEETTSDY
     DREKLQERLA KLAGGVAVIR VGGATEVEVK ERKDRVDDAM HATRAAVEEG ILPGGGVALL
     RASEHLKGIR TKNDDQKTGV EIVRKALSYP ARQIAINAGE DGSVIVGKIL EKDQYSYGYD
     SQTGEYGNLV SKGIIDPTKV VRVAIQNAAS VAALLITTEA MVAEVPKKNT GAGGMPPGGG
     GMGGMGGMDF
 
 
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