CH603_BRADU
ID CH603_BRADU Reviewed; 546 AA.
AC P35862;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Chaperonin GroEL 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=bll2059;
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], AND PROTEIN SEQUENCE OF 2-30.
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 [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=11157954; DOI=10.1128/jb.183.4.1405-1412.2001;
RA Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R.,
RA Hennecke H.;
RT "Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA
RT region of the Bradyrhizobium japonicum chromosome.";
RL J. Bacteriol. 183:1405-1412(2001).
RN [3]
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: By NifA.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z22603; CAA80316.1; -; Genomic_DNA.
DR EMBL; AF322013; AAG61029.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47324.1; -; Genomic_DNA.
DR PIR; S35311; S35311.
DR RefSeq; NP_768699.1; NC_004463.1.
DR RefSeq; WP_011084855.1; NZ_CP011360.1.
DR AlphaFoldDB; P35862; -.
DR SMR; P35862; -.
DR STRING; 224911.27350313; -.
DR PRIDE; P35862; -.
DR EnsemblBacteria; BAC47324; BAC47324; BAC47324.
DR GeneID; 64021824; -.
DR KEGG; bja:bll2059; -.
DR PATRIC; fig|224911.44.peg.1564; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR InParanoid; P35862; -.
DR OMA; SSAMFDK; -.
DR PhylomeDB; P35862; -.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8101485"
FT CHAIN 2..546
FT /note="Chaperonin GroEL 3"
FT /id="PRO_0000063296"
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 546 AA; 57785 MW; D09D4E2F236C87EB CRC64;
MSAKEVKFGV NARDRMLRGV DILANAVQVT LGPKGRNVVL DKSFGAPRIT KDGVAVAKEI
ELDDKFENMG AQMVREVASK AADAAGDGTT TATVLAAAIV REGAKSVAAG MNPMDLKRGI
DLAVEAVVAD LQKNSKKVTS NDEIAQVGAI SANGDQEIGK FLADAVKKVG NEGVITVEEA
KSLETELDVV EGMQFDRGYI SPYFVTNADK MRVEMDDAYI LINEKKLSSL NELLPLLEAV
VQTGKPLVIV AEDVEGEALA TLVVNRLRGG LKVAAVKAPG FGDRRKAMLQ DIAILTGGQA
ISEDLGIKLE NVTLNMLGRA KKVMIDKENT TIVNGAGKKA DIEARVAQIK AQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGATEVEVK ERKDRVDDAM HATRAAVEEG IVPGGGVALL
RASEQLKGLR TENDDQKTGV EIVRKALSWP ARQIAINAGE DGSIVVGKVL DNEQYSFGFD
AQTGEYSNLV SKGIIDPAKV VRIAVQNASS VAGLLITTEA MVAELPKKAT AGPAMPAAPG
MGGMDF
