CH60_ACET2
ID CH60_ACET2 Reviewed; 541 AA.
AC P48212; A3DJG1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
GN OrderedLocusNames=Cthe_2892;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9047357; DOI=10.1016/s0378-1119(96)00814-1;
RA Ciruela A., Cross S., Freedman R.B., Hazlewood G.P.;
RT "Sequence and transcriptional analysis of groES and groEL genes from the
RT thermophilic bacterium Clostridium thermocellum.";
RL Gene 186:143-147(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=8687408; DOI=10.1042/bj3160615;
RA Cross S.J., Ciruela A., Poomputsa K., Romaniec M.P.M., Freedman R.B.;
RT "Thermostable chaperonin from Clostridium thermocellum.";
RL Biochem. J. 316:615-622(1996).
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; Z68137; CAA92242.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN54090.1; -; Genomic_DNA.
DR PIR; S68249; S68249.
DR RefSeq; WP_003514589.1; NC_009012.1.
DR AlphaFoldDB; P48212; -.
DR SMR; P48212; -.
DR STRING; 203119.Cthe_2892; -.
DR EnsemblBacteria; ABN54090; ABN54090; Cthe_2892.
DR KEGG; cth:Cthe_2892; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_9; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000002145; 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; 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:8687408"
FT CHAIN 2..541
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063344"
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 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 15..16
FT /note="LE -> ML (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="Q -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 57474 MW; EDC8C71A3B28E789 CRC64;
MAKQIKFGEE ARRALERGVN QLADTVKVTL GPKGRNVVLD KKFGSPMITN DGVTIAKEIE
LEDPFENMGA QLVKEVATKT NDVAGDGTTT ATLLAQAIIR EGLKNVAAGA NPMLLKKGIA
KAVDAAVEGI KEISQKVKGK EDIARVASIS ANDEVIGELI ADAMEKVTND GVITVEEAKT
MGTNLEIVEG MQFDRGYVSP YMVTDTEKME AVLDEPYILI TDKKISNIQD ILPLLEQIVQ
QGKKLVIIAE DVEGEALATL LVNKLRGTFT CVAVKAPGFG DRRKAMLEDI AILTGGQVIT
SDLGLELKDT TVEQLGRARQ VKVQKENTII VDGAGDPKEI QKRIASIKSQ IEETTSDFDR
EKLQERLAKL AGGVAVIQVG AATETEMKEK KLRIEDALAA TKAAVEEGIV AGGGTALVNV
IPKVAKVLDT VSGDEKTGVQ IILRALEEPV RQIAENAGLE GSVIVEKVKA SEPGIGFDAY
NEKYVNMIEA GIVDPAKVTR SALQNAASVA SMVLTTESVV ADIPEKETSG GPGGAGMGGM
Y
