CH60_LISW6
ID CH60_LISW6 Reviewed; 542 AA.
AC A0AKH5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, 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=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}; OrderedLocusNames=lwe2089;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK21507.1; -; Genomic_DNA.
DR RefSeq; WP_011702848.1; NC_008555.1.
DR AlphaFoldDB; A0AKH5; -.
DR SMR; A0AKH5; -.
DR STRING; 386043.lwe2089; -.
DR PRIDE; A0AKH5; -.
DR EnsemblBacteria; CAK21507; CAK21507; lwe2089.
DR GeneID; 61189988; -.
DR KEGG; lwe:lwe2089; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_9; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000000779; 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.
FT CHAIN 1..542
FT /note="Chaperonin GroEL"
FT /id="PRO_1000025805"
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 476..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 542 AA; 57367 MW; 9818B45967C9F324 CRC64;
MAKDIKFSED ARRAMLRGVD QLANAVKVTL GPKGRNVVLE KKFGSPLITN DGVTIAKEIE
LEDPFENMGA KLVSEVASKT NDVAGDGTTT ATVLAQAMIQ EGLKNVTAGA NPVGVRRGIE
KAVATAIEEL KAISKPIESK ESIAQVAAIS SGDEEVGKLI AEAMERVGND GVITIEESKG
FATELDVVEG MQFDRGYTSP YMVTDSDKME AVLEKPYILI TDKKINNIQE ILPVLEQVVQ
QGRPMLIIAE DVEGEAQATL VLNKLRGTFN VVAVKAPGFG DRRKAMLEDI AILTGGQVIT
EDLGLELKTA TVDQLGTANK VVVTKDDTTI VEGAGDSTQI SARVNQIRAQ MEETTSEFDR
EKLQERLAKL AGGVAVVKVG AATETELKER KLRIEDALNS TRAAVEEGIV AGGGTALVSI
YNKVAALEAE GDVETGINIV LRSLEEPVRQ IAHNAGLEGS VIVERLKHEA VGVGFNAANG
EWVNMIDAGI VDPTKVTRSA LQNASSVAAL LLTTEAVVAD QPDENGPAAV PDMGMGGMGG
MM
