CH60_LACAC
ID CH60_LACAC Reviewed; 542 AA.
AC Q93G07; Q5FLX7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=LBA0406;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CRL 639;
RA Lorca G.L., Font de Valdez G.;
RT "Characterization of the Lactobacillus acidophilus CRL 639 groESL operon.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; AF300645; AAK97218.1; -; Genomic_DNA.
DR EMBL; CP000033; AAV42297.1; -; Genomic_DNA.
DR RefSeq; WP_003549158.1; NC_006814.3.
DR RefSeq; YP_193328.1; NC_006814.3.
DR AlphaFoldDB; Q93G07; -.
DR SMR; Q93G07; -.
DR STRING; 272621.LBA0406; -.
DR PRIDE; Q93G07; -.
DR EnsemblBacteria; AAV42297; AAV42297; LBA0406.
DR GeneID; 56942012; -.
DR KEGG; lac:LBA0406; -.
DR PATRIC; fig|272621.13.peg.392; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_9; -.
DR OMA; TDTDKME; -.
DR BioCyc; LACI272621:G1G49-400-MON; -.
DR Proteomes; UP000006381; 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..542
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063397"
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 477..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 170
FT /note="D -> E (in Ref. 1; AAK97218)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="I -> T (in Ref. 1; AAK97218)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="D -> E (in Ref. 1; AAK97218)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="K -> E (in Ref. 1; AAK97218)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="T -> TGKVT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 57820 MW; 498055D0C3513F2D CRC64;
MAKDIKFAEN ARRSLLKGVD KLADTVKTTI GPKGRNVVLE QSYGNPDITN DGVTIAKSIE
LKDHYENMGA KLVAEAAQKT NDIAGDGTTT ATVLTQAIAR EGMKNVTAGA NPVGIRRGIE
KATKAAVDEL HKISHKVESK EQIANVAAVS SASKEVGELI ADAMEKVGHD GVITIEDSRG
INTELSVVEG MQFDRGYLSQ YMVTDNDKME ADLDNPYILI TDKKISNIQD ILPLLQEIVQ
QGKSLLIIAD DVTGEALPTL VLNKIRGTFN VVAVKAPGFG DRRKAQLEDI AALTGGTVIT
DDLGFELKDT KIDQLGQARR VTVTKDSTTI VDGAGSKDAI KEREDSIRKQ IEESTSDFDK
KKLQERLAKL TGGVAVIHVG AATETELKER RYRIEDALNS TRAAVDEGYV AGGGTALVDV
EKAIKDLKGE TSDEQTGINI VLRALSAPVR QIAENAGKDG AVVLNKLESQ ENEIGYNAAT
DKWENMVEAG IIDPTKVTRT ALQNAASIAA LLLTTEAVVA DIPEDKPEAP QAGAAGAPGM
GM
