CH601_CERSP
ID CH601_CERSP Reviewed; 547 AA.
AC P20110; Q59773;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL1 {ECO:0000255|HAMAP-Rule:MF_00600};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HR;
RX PubMed=8990302; DOI=10.1128/jb.179.2.487-495.1997;
RA Lee W.T., Terlesky K.C., Tabita F.R.;
RT "Cloning and characterization of two groESL operons of Rhodobacter
RT sphaeroides: transcriptional regulation of the heat-induced groESL
RT operon.";
RL J. Bacteriol. 179:487-495(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=1982105; DOI=10.1016/0378-1097(90)90330-s;
RA Watson G.M.F., Mann N.H., McDonald G.A., Dunbar B.;
RT "Identification and characterization of a GroEL homologue in Rhodobacter
RT sphaeroides.";
RL FEMS Microbiol. Lett. 60:349-353(1990).
RN [3]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=1678280; DOI=10.1021/bi00247a013;
RA Terlesky K.C., Tabita F.R.;
RT "Purification and characterization of the chaperonin 10 and chaperonin 60
RT proteins from Rhodobacter sphaeroides.";
RL Biochemistry 30:8181-8186(1991).
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 heat shock.
CC -!- MISCELLANEOUS: This protein shows ATPase activity.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; U37369; AAB41336.1; -; Genomic_DNA.
DR RefSeq; WP_002719474.1; NZ_WTFI01000014.1.
DR AlphaFoldDB; P20110; -.
DR SMR; P20110; -.
DR GeneID; 67446081; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
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; 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; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1678280,
FT ECO:0000269|PubMed:1982105"
FT CHAIN 2..547
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000063512"
FT REGION 525..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 547 AA; 57950 MW; 8B2BFA7DA7BD2D57 CRC64;
MAAKDVKFDT DARDRMLRGV NILADAVKVT LGPKGRNVVI DKSFGAPRIT KDGVSVAKEI
ELSDKFENMG AQMVKEVASR TNDEAGDGTT TATVLAQAII KEGLKAVAAG MNPMDLKRGI
DLATSKVVEA IKAAARPVND SHEVAQVGTI SANGEAQIGR FIADAMQKVG NEGVITVEEN
KGLETEVEVV EGMQFDRGYL SPYFVTNADK MTAELDDVYI LLHEKKLSSL QPMVPLLEAV
IQSQKPLLII AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLQ DIAILTGGQV
ISEDLGMKLE NVTIDMLGRA KKISINKDNT TIVDGNGDKA EIDARVAQIR NQIEETSSDY
DREKLQERVA KLAGGVAVIR VGGMTEVEVK ERKDRVDDAL NATRAAVQEG IVVGGGVALI
QGGKALDGLT GENPDQNAGI TIVRRALEAP LRQIAQNAGV DGSVVAGKVR ESNEKSFGFN
AQTEEYGDMF KFGVIDPAKV VRTALEDAAS VASLLITTEA MIADKPEPKS PAGGPGMGGM
GGMDGMM
