CH60_LACJO
ID CH60_LACJO Reviewed; 543 AA.
AC Q9KJ23;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
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=LJ_0461;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11506 / JCM 1101 / NBRC 13952 / NCIMB 8795 / R-26 / VPI 11088;
RX PubMed=10388700; DOI=10.1128/aem.65.7.3033-3041.1999;
RA Walker D.C., Girgis H.S., Klaenhammer T.R.;
RT "The groESL chaperone operon of Lactobacillus johnsonii.";
RL Appl. Environ. Microbiol. 65:3033-3041(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AF214488; AAF75593.1; -; Genomic_DNA.
DR EMBL; AE017198; AAS08453.1; -; Genomic_DNA.
DR RefSeq; WP_004896780.1; NC_005362.1.
DR AlphaFoldDB; Q9KJ23; -.
DR SMR; Q9KJ23; -.
DR STRING; 257314.LJ_0461; -.
DR PRIDE; Q9KJ23; -.
DR EnsemblBacteria; AAS08453; AAS08453; LJ_0461.
DR GeneID; 66434769; -.
DR KEGG; ljo:LJ_0461; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_1_1_9; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000000581; 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:0046812; F:host cell surface binding; IDA:CAFA.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0098630; P:aggregation of unicellular organisms; IDA:CAFA.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IGI:CAFA.
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; 2.
DR SUPFAM; SSF52029; SSF52029; 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..543
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063399"
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 478..480
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"
FT CONFLICT 161
FT /note="A -> R (in Ref. 1; AAF75593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 57517 MW; 71AE6F998495F1AD CRC64;
MAKEIKFSEN ARHSLLKGVD KLADTVKTTL GPKGRNVVLE KSYGAPDITN DGVTIAKSIE
LENHFENMGA KLVSEAAQKT NDIAGDGTTT ATVLTQAIVR EGMKNVTAGA NPVGIRRGIE
TATKAAVDEL HKISHKVSTK DEIAQVASVS SASTEVGNLI ADAMEKVGHD GVITIEESKG
IDTELSVVEG MQFDRGYLSQ YMVTDNDKME ADLDNPYILI TDKKISNIQD ILPLLQEIVQ
QGKSLLIIAD DVDGEALPTL VLNKIRGTFN VVAVKAPGFG DRRKAMLEDI AILTGGTVIS
SDLGLELKDT KIDQLGKAGK VTVTKDSTTI VEGAGSKEAI AERVDQIKKQ IADTTSDFDR
EKLQERLAKL AGGVAVIKVG AATETELKER KYRIEDALNA TRAAVEEGYV AGGGTALVDV
MKSIQGTVKG DSEDAETGVK IVMKALGAPV RQIAENAGKD GAVILDHLEH EDPEVGYNAA
TNKWENMVKA GIIDPTKVTR SALQNAASIA ALLLTTEAVV ADAPEDDKNQ APAAPNPGMG
MGM
