CH60_CITK8
ID CH60_CITK8 Reviewed; 548 AA.
AC A8AMQ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=CKO_03692;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV14769.1; -; Genomic_DNA.
DR RefSeq; WP_012134466.1; NC_009792.1.
DR AlphaFoldDB; A8AMQ6; -.
DR BMRB; A8AMQ6; -.
DR SMR; A8AMQ6; -.
DR STRING; 290338.CKO_03692; -.
DR EnsemblBacteria; ABV14769; ABV14769; CKO_03692.
DR GeneID; 45137395; -.
DR KEGG; cko:CKO_03692; -.
DR HOGENOM; CLU_016503_3_0_6; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000008148; 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..548
FT /note="Chaperonin GroEL"
FT /id="PRO_1000025770"
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 479..481
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 548 AA; 57408 MW; B6ACFB22277F76A8 CRC64;
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQSII TEGLKAVAAG MNPMDLKRGI
DKAVAAAVEE LKTLSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG
TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV
ISEEIGMELE KSTLEDLGQA KRVVINKDTT TIIDGVGEES AIQGRVTQIR QQIEEATSDY
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI
RVASKIAELK GQNEDQNVGI KVALRAMESP LRQIVLNCGE EPSVVANTVK SGDGNYGYNA
ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKGDAP DLGAAGGMGG
MGGMGGMM