CH60_STRP6
ID CH60_STRP6 Reviewed; 543 AA.
AC Q5X9L8; P82485;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
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=M6_Spy1760;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-12; 72-79; 105-131; 141-152; 167-195; 225-264;
RP 276-284; 321-343; 392-402; 424-442 AND 488-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=JRS4 / Serotype M6;
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (MAY-2000) to UniProtKB.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT87895.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000003; AAT87895.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002982320.1; NC_006086.1.
DR AlphaFoldDB; Q5X9L8; -.
DR SMR; Q5X9L8; -.
DR EnsemblBacteria; AAT87895; AAT87895; M6_Spy1760.
DR GeneID; 57853427; -.
DR KEGG; spa:M6_Spy1760; -.
DR HOGENOM; CLU_016503_3_0_9; -.
DR Proteomes; UP000001167; 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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..543
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063560"
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 476..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 543 AA; 57065 MW; F2D07B79B6FD6C89 CRC64;
MAKDIKFSAD ARAAMVRGVD MLADTVKVTL GPKGRNVVLE KAFGSPLITN DGVTIAKEIE
LEDHFENMGA KLVSEVASKT NDIAGDGTTT ATVLTQAIVH EGLKNVTAGA NPIGIRRGIE
TATATAVEAL KAIAQPVSGK EAIAQVAAVS SRSEKVGEYI SEAMERVGND GVITIEESRG
METELEVVEG MQFDRGYLSQ YMVTDNEKMV ADLENPFILI TDKKVSNIQD ILPLLEEVLK
TNRPLLIIAD DVDGEALPTL VLNKIRGTFN VVAVKAPGFG DRRKAMLEDI AILTGGTVIT
EDLGLELKDA TMTALGQAAK ITVDKDSTVI VEGSGSSEAI ANRIALIKSQ LETTTSDFDR
EKLQERLAKL AGGVAVIKVG APTETALKEM KLRIEDALNA TRAAVEEGIV AGGGTALITV
IEKVAALELE GDDATGRNIV LRALEEPVRQ IALNAGYEGS VVIDKLKNSP AGTGFNAATG
EWVDMIKTGI IDPVKVTRSA LQNAASVASL ILTTEAVVAN KPEPAAPAPA MPAGMDPGMM
GGF
