ID CH602_BRASB Reviewed; 541 AA.
AC A5EET6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=BBta_2521;
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=288000;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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}.
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DR EMBL; CP000494; ABQ34680.1; -; Genomic_DNA.
DR RefSeq; WP_012042708.1; NC_009485.1.
DR AlphaFoldDB; A5EET6; -.
DR SMR; A5EET6; -.
DR STRING; 288000.BBta_2521; -.
DR KEGG; bbt:BBta_2521; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OrthoDB; 9766614at2; -.
DR Proteomes; UP000000246; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1.
DR HAMAP; MF_00600; CH60; 1.
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 NCBIfam; TIGR02348; GroEL; 1.
DR PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..541
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000331975"
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 541 AA; 57257 MW; 4115B23EBFF87791 CRC64;
MSAKDVKFAA DARERLIRGV DILANAVKVT LGPKGRNVLI EKSFGAPRIT KDGVTVAKEI
ELEDKYENLG AQLLRQVASK TNDLAGDGTT TATVLAQAIV REGAKAVAAS LNPLDLKRGI
DLAVAEAIKD IEKRARKVQS SEEVAQVGTI SANSDAAVGK IIATAVKKVG NDGVITVEEA
KSLETELDVV EGLQFDRGYL SPYFVTNSDK LLVEFEEPYI LIHESKLTSL QPLLPVLEAV
VQTGRPLLVI AEDVEGEALA TLVVNKLRGG LKVAAVKAPG FGDRRKAQLE DIAILTGGQT
ISQDLGIKLE NVTLSQLGRA RRIRIDKENT TVVGGTGKKK DIDARIAQIR AQIEETTSDY
DREKLQERLA KLSGGVAVIR VGGATEVEVK EKKDRVDDAL NATRAAIAEG IVPGGGVALL
RAKAAVSKLT NPNPDIQAGI QIVLKALEAP IRQIADNAGV EGSIVVGKIL ENRSPTFGFD
AQKEEYVDLI EAGIVDPAKV VRTALQDAAS VAALIVTTEA LVVELPKEKA ALPAAGAGAD
F
//
