CH60_MYCAV
ID CH60_MYCAV Reviewed; 151 AA.
AC Q48900; Q48885; Q48886; Q48887; Q48901; Q53491;
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 Mycobacterium avium.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=234, and 368;
RA Ros C., Belak K.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-138.
RC STRAIN=88-1107, 89-1177, 89-615, and TMH16;
RX PubMed=7848059;
RA Kapur V., Li L.L., Hamrick M.R., Plikaytis B.B., Shinnick T.M., Telenti A.,
RA Jacobs W.R. Jr., Banerjee A., Cole S., Yuen K.Y., Clarridge J.E.,
RA Kreiswirth B.N., Musser J.M.;
RT "Rapid Mycobacterium species assignment and unambiguous identification of
RT mutations associated with antimicrobial resistance in Mycobacterium
RT tuberculosis by automated DNA sequencing.";
RL Arch. Pathol. Lab. Med. 119:131-138(1995).
RN [3]
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; U55826; AAC44449.1; -; Genomic_DNA.
DR EMBL; U55827; AAC44450.1; -; Genomic_DNA.
DR EMBL; U17922; AAB39042.1; -; Genomic_DNA.
DR EMBL; U17923; AAB39043.1; -; Genomic_DNA.
DR EMBL; U17924; AAB39896.1; -; Genomic_DNA.
DR EMBL; S76642; AAP31977.1; -; Genomic_DNA.
DR PIR; S05294; S05294.
DR AlphaFoldDB; Q48900; -.
DR SMR; Q48900; -.
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_0000063422"
FT BINDING 41..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT VARIANT 50
FT /note="A -> G (in strain: TMH16)"
FT VARIANT 121
FT /note="K -> N (in strain: TMH16)"
FT VARIANT 136
FT /note="F -> S (in strain: TMH16)"
FT NON_TER 1
FT NON_TER 151
SQ SEQUENCE 151 AA; 15827 MW; 9B52220C5AD32007 CRC64;
PTITNDGVSI AKEIELEDPY EKIGAELVKE VAKKTDDVAG DGTTTATVLA QALVREGLRN
VAAGANPLGL KRGIEKAVEK VTETLLKSAK EVETKDQIAA TAAISAGDQS IGDLIAEAMD
KVGNEGVITV EESNTFGLQL ELTEGMRFDK G
