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CH604_BRADU
ID   CH604_BRADU             Reviewed;         543 AA.
AC   Q89P00;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chaperonin GroEL 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groEL, groL4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=blr3683;
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 [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   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000305}.
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DR   EMBL; BA000040; BAC48948.1; -; Genomic_DNA.
DR   RefSeq; NP_770323.1; NC_004463.1.
DR   RefSeq; WP_011086464.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89P00; -.
DR   SMR; Q89P00; -.
DR   STRING; 224911.27351943; -.
DR   EnsemblBacteria; BAC48948; BAC48948; BAC48948.
DR   GeneID; 64023415; -.
DR   KEGG; bja:blr3683; -.
DR   PATRIC; fig|224911.44.peg.3347; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_5; -.
DR   InParanoid; Q89P00; -.
DR   OMA; GYLSHHM; -.
DR   PhylomeDB; Q89P00; -.
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   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   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..543
FT                   /note="Chaperonin GroEL 4"
FT                   /id="PRO_0000063297"
FT   BINDING         29..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         86..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         476..478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   543 AA;  56659 MW;  555F36077A6C5574 CRC64;
     MPKVLLHDIE ARRALARGVQ KLAAAIESTL GPKGMNAMVD RPIGTPIVSR DGVTIASEIE
     LPDRFENMGA QVVREVSMQT NEVAGDGTTT AMVLANGLIQ GGVAALERGA KAVDLCKGID
     RAVEVVVESL KSAAIPVSDR RTLQAVATIA STDSHLGDLI AEAVERVGKD GIISSDYGLT
     TSTTLEVVEG MSFDRGYISH HMVTDVEKME VVLEQPYILL TDLKIKAPGE LAAVRARVAE
     TGKPLVIVAE EIAPEVVVTL LGEGNRGKVL VVNPPDYGHW RKAMMDDLAI ITGGRVIARE
     LGGMLEEASL ADLGTARQVR ASARETVIIR GGGDDAAIAA RRQQVAKQHD LAPPNIEQDK
     LKERLAKLSG GTAVIFAGGV TPVEQKRTIQ LIDDALSAAR AAAEEGIVPG GGTALAQCAP
     VVVRALGNIN GDLGEGIKLV RETLSRPAAF IARNAGHDAA KVVAELQSSR AGVGFDAANG
     VFIDMVSAGI VDPVRVTYTA LRNAASVATL VLTTNTLVAD VPEYVDPTQG PALGGGAEKL
     GRA
 
 
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