ID CH60_AERS4 Reviewed; 544 AA.
AC A4SR80;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
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};
GN OrderedLocusNames=ASA_3431;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO91402.1; -; Genomic_DNA.
DR RefSeq; WP_005318975.1; NC_009348.1.
DR AlphaFoldDB; A4SR80; -.
DR SMR; A4SR80; -.
DR STRING; 29491.GCA_000820065_04368; -.
DR KEGG; asa:ASA_3431; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_6; -.
DR Proteomes; UP000000225; 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; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 NCBIfam; TIGR02348; GroEL; 1.
DR PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..544
FT /note="Chaperonin GroEL"
FT /id="PRO_1000025749"
FT BINDING 30..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 87..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 544 AA; 57320 MW; C40F7C207B61F690 CRC64;
MAAKEVKFGN EARIKMLEGV NILADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
ELEDKFQNMG AQMVKEVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI
DKAVIAAVAE LQVLSQPCAD NNAIAQVGTI SANSDEKVGR LIAEAMDKVG RDGVITVEDG
QGLDDELAVV EGMQFDRGYL SPYFVNKPET GAVELDDPFI LLVDKKVSNI REMLPVLEGV
AKAGKPLLIV AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIAMLTGGTV
ISEEVGMELE KATLEDLGRA KRIVITKENT TIIDGVGDAA LIESRVAQIR QQIEETSSDY
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVDDAL HATRAAVEEG VVAGGGVALV
RVAAKLAGLR GDNEDQNVGI KVALRAMEAP LRQIVINAGE EASVIANAVK NGEGNFGYNA
YTEQYGDMLA MGILDPTKVT RSALQFASSI AGLMITTECM ITELPKKDTP AMPDMGGMGG
MGMM
//
