CH60_CLODI
ID CH60_CLODI Reviewed; 540 AA.
AC Q9KKF0; Q9KJV7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
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};
OS Clostridioides difficile (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=1496;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=79-685, and ATCC 43603 / CCUG 37787 / 5036;
RX PubMed=11160803; DOI=10.1099/00221287-147-1-87;
RA Hennequin C., Porcheray F., Waligora-Dupriet A.-J., Collignon A.,
RA Barc M.-C., Bourlioux P., Karjalainen T.;
RT "GroEL (Hsp60) of Clostridium difficile is involved in cell adherence.";
RL Microbiology 147:87-96(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; AF080547; AAF73984.1; -; Genomic_DNA.
DR EMBL; AF159449; AAF80372.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KKF0; -.
DR SMR; Q9KKF0; -.
DR MoonProt; Q9KKF0; -.
DR PRIDE; Q9KKF0; -.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
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:0044650; P:adhesion of symbiont to host cell; IDA:CACAO.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:CAFA.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0010447; P:response to acidic pH; IMP:CAFA.
DR GO; GO:0009408; P:response to heat; IMP:CAFA.
DR GO; GO:1990641; P:response to iron ion starvation; IMP:CAFA.
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.
FT CHAIN 1..540
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063340"
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 VARIANT 214
FT /note="N -> K (in strain: ATCC 43603)"
FT VARIANT 235
FT /note="L -> V (in strain: ATCC 43603)"
FT VARIANT 327
FT /note="S -> N (in strain: ATCC 43603)"
FT VARIANT 339
FT /note="A -> S (in strain: ATCC 43603)"
SQ SEQUENCE 540 AA; 57677 MW; 7D19C198D1091166 CRC64;
MAKEIKFSEE TRRALEAGVN KLADTVKVTL GPKGRNVILD KKFGSPLITN DGVTIAKEIE
LEDRFENMGA QLVKEVATKT NDVAGDGTTT ATVLAQAIIR EGLKNVTAGA NPILLRKGIQ
KAVTVAVEEL KNQSRIVETQ EAISQVASIS AGDEEVGKLI AEAMEIVGKD GVITVEESQT
MNTELDAVEG MQFDRGFVSA YMVTDVDKME AVLNDPYILI TDKKISNIQE LLPVLEQIVQ
QGKKLLIIAE DVEGEALSTL VVNKLRGTFD VVAVKAPGFG DRRKEMLQDI AILTGAQVIS
EELGYDLKEA DLSMLGRASS VKVTKESTTI VDGSGDKKAI EDRVTQIKHQ VEQTTSDFDR
EKLMERLAKL AGGVAVVKVG AATEVELKER KLRIEDALNA TRAAVEEGIV AGGGTAFVSV
IPAIGTLIES LEGEVKLGAQ IVKKALEEPL RQIAINAGLE GAVIVQNVVN SEAETGFDAL
NEKYVNMIEA GIVDPTKVSR SALQNAASIA STFLTTEAAV ADLPEKEDAG MPGTGMDGMY
