CH601_MYCLE
ID CH601_MYCLE Reviewed; 537 AA.
AC P37578;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groE1, groL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=ML0381; ORFNames=B1620_C3_228, B229_C3_248;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1354834; DOI=10.1111/j.1365-2958.1992.tb01372.x;
RA de Wit T.F.R., Bekelie S., Osland A., Miko T.L., Hermans P.W.M.,
RA van Soolingen D., Drijfhout J., Schoeningh R., Janson A.A.M., Thole J.E.R.;
RT "Mycobacteria contain two groEL genes: the second Mycobacterium leprae
RT groEL gene is arranged in an operon with groES.";
RL Mol. Microbiol. 6:1995-2007(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; Z11665; CAB62574.1; -; Genomic_DNA.
DR EMBL; U00015; AAC43228.1; -; Genomic_DNA.
DR EMBL; U00020; AAA17312.1; -; Genomic_DNA.
DR EMBL; AL583918; CAC29889.1; -; Genomic_DNA.
DR PIR; S25181; S25181.
DR RefSeq; NP_301373.1; NC_002677.1.
DR RefSeq; WP_010907697.1; NC_002677.1.
DR AlphaFoldDB; P37578; -.
DR SMR; P37578; -.
DR STRING; 272631.ML0381; -.
DR EnsemblBacteria; CAC29889; CAC29889; CAC29889.
DR KEGG; mle:ML0381; -.
DR PATRIC; fig|272631.5.peg.643; -.
DR Leproma; ML0381; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_11; -.
DR OMA; YWIASNA; -.
DR Proteomes; UP000000806; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..537
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000063436"
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"
SQ SEQUENCE 537 AA; 55816 MW; F2355B1BCFAED50F CRC64;
MSKLIEYDET ARHAMEVGMN KLADTVRVTL GPRGRHVVLA KAFGGPTITN DGVTVAREID
LEDPFENLGA QLVKSVATKT NDVAGDGTTT ATVLAQALVK GGLRMVAAGA NPVALGAGIS
KAADAVSEAL LAVATPVAGK DAITQVATVS SRDEQIGALV GEGMNKVGTD GVVSVEESST
LDTELEFTEG VGFDKGFLSA YFVTDFDSQQ AVLDDPLVLL HQEKISSLPE LLPMLEKVTE
SGKPLLIVAE DLEGEALATL VVNSIRKTLK AVAVKSPFFG DRRKAFLEDL AIVTGGQVVN
PETGLVLREV GTDVLGSARR VVVSKDDTII VDGGGSNDAV AKRVNQLRAE IEVSDSEWDR
EKLQERVAKL AGGVAVIKVG AVTETALKKR KESVEDAVAA AKASIEEGII AGGGSALVQC
GAALKQLRTS LTGDEALGID VFFEALKAPL YWIATNAGLD GAVVVDKVSG LPAGHGLNAS
TLGYGDLVAD GVVDPVKVTR SAVLNAASVA RMMLTTETAV VDKPAKTEEH DHHGHAH
