CH60_LACLA
ID CH60_LACLA Reviewed; 542 AA.
AC P37282;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
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}, mopA;
GN OrderedLocusNames=LL0394; ORFNames=L198893;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8486277; DOI=10.1016/0378-1119(93)90626-e;
RA Kim S.G., Batt C.A.;
RT "Cloning and sequencing of the Lactococcus lactis subsp. lactis groESL
RT operon.";
RL Gene 127:121-126(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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; X71132; CAA50446.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK04492.1; -; Genomic_DNA.
DR PIR; B86674; B86674.
DR PIR; JN0661; JN0661.
DR PIR; S32106; S32106.
DR RefSeq; NP_266550.1; NC_002662.1.
DR RefSeq; WP_003131585.1; NC_002662.1.
DR AlphaFoldDB; P37282; -.
DR SMR; P37282; -.
DR STRING; 272623.L198893; -.
DR MoonProt; P37282; -.
DR PaxDb; P37282; -.
DR EnsemblBacteria; AAK04492; AAK04492; L198893.
DR KEGG; lla:L198893; -.
DR PATRIC; fig|272623.7.peg.428; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_9; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
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:2001065; F:mannan binding; IDA:CAFA.
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..542
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063400"
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"
FT CONFLICT 63
FT /note="D -> V (in Ref. 1; CAA50446)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="T -> N (in Ref. 1; CAA50446)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="D -> H (in Ref. 1; CAA50446)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="L -> V (in Ref. 1; CAA50446)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="M -> I (in Ref. 1; CAA50446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 57201 MW; D7D6F5319DA59721 CRC64;
MSKDIKFSSD ARTAMMRGID ILADTVKTTL GPKGRNVVLE KSYGSPLITN DGVTIAKEIE
LEDHFENMGA KLVSEVASKT NDIAGDGTTT ATVLTQAIVR EGLKNVTAGA NPVGIRRGIE
LAAETAVASI KEMAIPVHDK SAIAQVATVS SRSEKVGEYI SDAMERVGSD GVITIEESKG
MQTELDVVEG MQFDRGYLSQ YMVSNTEKMV AELDNPYILI TDKKISNIQE ILPLLEQILK
TNRPLLIVAD DVDGEALPTL VLNKIKGVFN VVAVKAPGFG DRRKAQLEDL AILTGGTVIT
EELGLDLKDA TLEALGQAAK ATVDKDHTTI VEGAGSADAI SDRVAIIKAQ IEKTTSDFDR
EKLQERLAKL AGGVAVVKVG AATETELKAM KLLIEDALNA TRAAVEEGIV SGGGTALVNA
IAALDKLSEE GDIQTGINIV RRALEEPVRQ IAANAGYEGS VIIDKLRSEE VGTGFNAATG
QWVNMIEEGI VDPAKVTRSA LQNAASVAGL ILTTEAVVAN KPEPAAPAMP PMDPSMGMGG
MM
