CH60_MYCCH
ID CH60_MYCCH Reviewed; 151 AA.
AC Q49093; Q53494;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=65 kDa heat shock protein;
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Flags: Fragment;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
OS Mycobacteroides chelonae (Mycobacterium chelonae).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides.
OX NCBI_TaxID=1774;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14472 / DSM 43283 / Magnussen 921;
RA Ros C., Belak K.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-133.
RX PubMed=7699930;
RA Hidaka E., Ueno I., Kawakami Y., Furuwatari C., Furihata K., Katsuyama T.;
RT "Detection and identification of mycobacteria by PCR-RFLP method.";
RL Rinsho Byori 43:155-161(1995).
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, ECO:0000305}.
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DR EMBL; U55832; AAC44452.1; -; Genomic_DNA.
DR EMBL; S76648; AAP31980.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49093; -.
DR SMR; Q49093; -.
DR STRING; 1774.GR01_03075; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Stress response.
FT CHAIN <1..>151
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063425"
FT BINDING 41..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 126
FT /note="G -> A (in Ref. 2; AAP31980)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 151
SQ SEQUENCE 151 AA; 15799 MW; 3890DE261EF57436 CRC64;
PTITNDGVSI AKEIELEDPY EKIGAELVKE VAKKTDDVAG DGTTTATVLA QALVKEGLRN
VAAGANPLGL KRGIEKAVEK VTETLLKSAK EVETKEQIAA TAGISAGDQS IGDLIAEAMD
KVGNEGVITV EESNTFGLQL ELTEGMRFDK G
