CH60_EHRRW
ID CH60_EHRRW Reviewed; 551 AA.
AC P48213; Q5FDA8; Q5HAN8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
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}, mopA;
GN OrderedLocusNames=Erum6420, ERWE_CDS_06730;
OS Ehrlichia ruminantium (strain Welgevonden).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=254945;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7496520; DOI=10.1099/13500872-141-9-2091;
RA Lally N.C., Nicoll S., Paxton E.A., Cary C.M., Sumption K.J.;
RT "The Cowdria ruminantium groE operon.";
RL Microbiology 141:2091-2100(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA Allsopp B.A.;
RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT tandem repeats of actively variable copy number.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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; U13638; AAA93153.1; -; Genomic_DNA.
DR EMBL; CR767821; CAH58374.1; -; Genomic_DNA.
DR EMBL; CR925678; CAI27167.1; -; Genomic_DNA.
DR RefSeq; WP_011155322.1; NC_006832.1.
DR AlphaFoldDB; P48213; -.
DR SMR; P48213; -.
DR STRING; 254945.Erum6420; -.
DR PRIDE; P48213; -.
DR EnsemblBacteria; CAI27167; CAI27167; ERWE_CDS_06730.
DR GeneID; 56785404; -.
DR KEGG; eru:Erum6420; -.
DR KEGG; erw:ERWE_CDS_06730; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; TDTDKME; -.
DR BioCyc; ERUM254945:ERUM_RS03480-MON; -.
DR Proteomes; UP000001021; 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.
FT CHAIN 1..551
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063365"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 50
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 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 487
FT /note="M -> T (in Ref. 1; AAA93153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 58859 MW; 8446286E28E4E277 CRC64;
MANMVVTGEQ LDKSIREVVR ILEDAVGCTA GPKGLTVAIS KPYGAPEVTK DGYKVMKSIK
PEDPLALAIA NIIAQSASQC NDKVGDGTTT CSILTAKVIE EVSKVKAAGA DIICVREGVL
KAKEAVLEAL KCMKREVLSE EEIAQVATIS ANGDKNIGTK IAQCVKEVGK DGVITVEESK
GFKELDVEKT DGMQFDRGYL SPYFVTNSEK MLVEFENPYI LLTEKKLNII QPLLPILENI
ARSGRPLLII AEDVEGEALS TLVLNKLRGG LHVAAVKAPG FGDRRKDMLG DIAILTGAKH
VINDELAIKM EDLTLCDLGT AKNIRITKDT TTIIGSVDNS CAHVQSRICQ IRMQIDNSTS
DYDKEKLQER LAKLSGGVAV LKVGGSSEVE VKERKDRVED ALHATRAAVE EGVVPGGGAA
LLYTLSALDN LKSKNDDEQL GINIVKRALQ APIKRIIKNA GSENAPCVIA HLLKQNDKEL
IFNVDVMNFA NAFTSGVIDP LKVVRIAFDF AVSLAAVFMT LNAIVVDIPS KDDNSAAGGA
GMGGMGGMGG F
