CH60_CHLMU
ID CH60_CHLMU Reviewed; 544 AA.
AC Q59322; P56837;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
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=TC_0386;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MoPn;
RX PubMed=7909303; DOI=10.1016/0378-1119(94)90145-7;
RA Ho Y., Zhang Y.-X.;
RT "The sequence of the groES and groEL genes from the mouse pneumonitis agent
RT of Chlamydia trachomatis.";
RL Gene 141:143-144(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MoPn;
RX PubMed=8955323; DOI=10.1128/jb.178.23.6983-6990.1996;
RA Tan M., Wong B., Engel J.N.;
RT "Transcriptional organization and regulation of the dnaK and groE operons
RT of Chlamydia trachomatis.";
RL J. Bacteriol. 178:6983-6990(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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 stress.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; L12004; AAA19871.1; -; Genomic_DNA.
DR EMBL; U52049; AAA97911.1; -; Genomic_DNA.
DR EMBL; AE002160; AAF39243.1; -; Genomic_DNA.
DR PIR; D81709; D81709.
DR PIR; I40731; I40731.
DR RefSeq; WP_010230304.1; NZ_CP027217.1.
DR AlphaFoldDB; Q59322; -.
DR SMR; Q59322; -.
DR STRING; 243161.TC_0386; -.
DR EnsemblBacteria; AAF39243; AAF39243; TC_0386.
DR GeneID; 1245738; -.
DR KEGG; cmu:TC_0386; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_0; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000000800; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063327"
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 481..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 387
FT /note="I -> N (in Ref. 1; AAA19871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 58106 MW; 3C7660523E0B2701 CRC64;
MVAKNIKYNE EARKKIQKGV KTLAEAVKVT LGPKGRHVVI DKSFGSPQVT KDGVTVAKEV
ELADKHENMG AQMVKEVASK TADKAGDGTT TATVLAEAIY TEGLRNVTAG ANPMDLKRGI
DKAVKVVVDQ IKKISKPVQH HKEIAQVATI SANNDAEIGN LIAEAMEKVG KNGSITVEEA
KGFETVLDVV EGMNFNRGYL SSYFATNPET QECVLEDALV LIYDKKISGI KDFLPVLQQV
AESGRPLLII AEDIEGEALA TLVVNRIRGG FRVCAVKAPG FGDRRKAMLE DIAILTGGQL
ISEELGMKLE NASLAMLGKA KKVIVSKEDT TIVEGMGEKE ALDARCESIK KQIEDSTSDY
DKEKLQERLA KLSGGVAVIR VGAATEIEMK EKKDRVDDAQ HATIAAVEEG ILPGGGTALI
RCIPTLEAFL PMLTNEDERI GARIVLKALS APLKQIAANA GKEGAIIFQQ VMSRSANEGY
DALRDAYTDM IEAGILDPAK VTRSALESAA SVAGLLLTTE ALIAEIPEEK PAAAPAMPGA
GMDY
