CH60_CHLTR
ID CH60_CHLTR Reviewed; 544 AA.
AC P0C0Z7; O84112; P17203;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
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}, hypB, mopA;
GN OrderedLocusNames=CT_110;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L2;
RX PubMed=1987066; DOI=10.1128/iai.59.1.79-90.1991;
RA Cerrone M.C., Ma J.J., Stephens R.S.;
RT "Cloning and sequence of the gene for heat shock protein 60 from Chlamydia
RT trachomatis and immunological reactivity of the protein.";
RL Infect. Immun. 59:79-90(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-11.
RA Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M.,
RA Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G.,
RA Pallini V.;
RL Submitted (SEP-1994) to UniProtKB.
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; M58027; AAA23128.1; -; Genomic_DNA.
DR EMBL; AE001273; AAC67701.1; -; Genomic_DNA.
DR PIR; A71555; A71555.
DR PIR; B41479; B41479.
DR RefSeq; NP_219613.1; NC_000117.1.
DR RefSeq; WP_010725062.1; NC_000117.1.
DR AlphaFoldDB; P0C0Z7; -.
DR SMR; P0C0Z7; -.
DR STRING; 813.O172_00595; -.
DR EnsemblBacteria; AAC67701; AAC67701; CT_110.
DR GeneID; 884030; -.
DR KEGG; ctr:CT_110; -.
DR PATRIC; fig|272561.5.peg.120; -.
DR HOGENOM; CLU_016503_3_0_0; -.
DR InParanoid; P0C0Z7; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000000431; 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; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063332"
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 VARIANT 124
FT /note="V -> A (in strain: L2)"
FT VARIANT 131
FT /note="I -> V (in strain: L2)"
FT VARIANT 132
FT /note="R -> K (in strain: L2)"
FT VARIANT 189
FT /note="I -> V (in strain: L2)"
FT VARIANT 191
FT /note="E -> D (in strain: L2)"
FT VARIANT 217
FT /note="D -> E (in strain: L2)"
FT VARIANT 255
FT /note="E -> V (in strain: L2)"
FT VARIANT 264
FT /note="V -> G (in strain: L2)"
FT VARIANT 289
FT /note="L -> F (in strain: L2)"
FT CONFLICT 4
FT /note="K -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 58147 MW; 2CE404C5BBE6E623 CRC64;
MVAKNIKYNE EARKKIQKGV KTLAEAVKVT LGPKGRHVVI DKSFGSPQVT KDGVTVAKEV
ELADKHENMG AQMVKEVASK TADKAGDGTT TATVLAEAIY TEGLRNVTAG ANPMDLKRGI
DKAVKVVVDQ IRKISKPVQH HKEIAQVATI SANNDAEIGN LIAEAMEKVG KNGSITVEEA
KGFETVLDIV EGMNFNRGYL SSYFATNPET QECVLEDALV LIYDKKISGI KDFLPVLQQV
AESGRPLLII AEDIEGEALA TLVVNRIRGG FRVCAVKAPG FGDRRKAMLE DIAILTGGQL
ISEELGMKLE NANLAMLGKA KKVIVSKEDT TIVEGMGEKE ALEARCESIK KQIEDSSSDY
DKEKLQERLA KLSGGVAVIR VGAATEIEMK EKKDRVDDAQ HATIAAVEEG ILPGGGTALI
RCIPTLEAFL PMLTNEDEQI GARIVLKALS APLKQIAANA GKEGAIIFQQ VMSRSANEGY
DALRDAYTDM LEAGILDPAK VTRSALESAA SVAGLLLTTE ALIAEIPEEK PAAAPAMPGA
GMDY
