CH60_NEORS
ID CH60_NEORS Reviewed; 548 AA.
AC P48214; O34196; O52314; O52315; O52316; O52317; O52392;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 97.
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;
OS Neorickettsia risticii (Ehrlichia risticii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=950;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-409.
RX PubMed=9230387; DOI=10.1128/jcm.35.8.2087-2092.1997;
RA Sumner J.W., Nicholson W.L., Massung R.F.;
RT "PCR amplification and comparison of nucleotide sequences from the groESL
RT heat shock operon of Ehrlichia species.";
RL J. Clin. Microbiol. 35:2087-2092(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-548.
RC STRAIN=90-12;
RA Vemulapalli R., Biswas B., Dutta S.K.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-319.
RC STRAIN=Various strains;
RX PubMed=9687446; DOI=10.1128/aem.64.8.2888-2893.1998;
RA Barlough J.E., Reubel G.H., Madigan J.E., Vredevoe L.K., Miller P.E.,
RA Rikihisa Y.;
RT "Detection of Ehrlichia risticii, the agent of Potomac horse fever, in
RT freshwater stream snails (Pleuroceridae: Juga spp.) from Northern
RT California.";
RL Appl. Environ. Microbiol. 64:2888-2893(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-319.
RC STRAIN=Various strains;
RX PubMed=9620368; DOI=10.1128/jcm.36.6.1501-1511.1998;
RA Reubel G.H., Barlough J.E., Madigan J.E.;
RT "Production and characterization of Ehrlichia risticii, the agent of
RT potomac horse fever, from snails (Pleuroceridae: Juga spp) in aquarium
RT culture and genetic comparison to equine strains.";
RL J. Clin. Microbiol. 36:1501-1511(1998).
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; U96732; AAB65633.1; -; Genomic_DNA.
DR EMBL; U24396; AAA65602.1; -; Genomic_DNA.
DR EMBL; AF037212; AAB95414.1; -; Genomic_DNA.
DR EMBL; AF037213; AAB95415.1; -; Genomic_DNA.
DR EMBL; AF037214; AAB95416.1; -; Genomic_DNA.
DR EMBL; AF036660; AAC01584.1; -; Genomic_DNA.
DR EMBL; AF036661; AAC01585.1; -; Genomic_DNA.
DR EMBL; AF036662; AAC01586.1; -; Genomic_DNA.
DR EMBL; AF036663; AAC01587.1; -; Genomic_DNA.
DR EMBL; AF036664; AAC01588.1; -; Genomic_DNA.
DR EMBL; AF036665; AAC01589.1; -; Genomic_DNA.
DR EMBL; AF036666; AAC01590.1; -; Genomic_DNA.
DR EMBL; AF036667; AAC01591.1; -; Genomic_DNA.
DR EMBL; AF036668; AAC01592.1; -; Genomic_DNA.
DR EMBL; AF036669; AAC01593.1; -; Genomic_DNA.
DR EMBL; AF036670; AAC01594.1; -; Genomic_DNA.
DR AlphaFoldDB; P48214; -.
DR SMR; P48214; -.
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..548
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063364"
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 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT VARIANT 163
FT /note="E -> K (in strain: SHSN-2)"
FT VARIANT 205
FT /note="I -> T (in strain: Danny/horse/Oregon)"
FT VARIANT 209
FT /note="E -> G (in strain: Thorenberg/horse/Oregon)"
FT VARIANT 235
FT /note="P -> S (in strain: Stagnicola/snail/Oregon)"
FT VARIANT 277
FT /note="K -> N (in strain: Drpepper/horse/California)"
FT VARIANT 299
FT /note="K -> R (in strain: Stagnicola/snail/Oregon)"
FT CONFLICT 60
FT /note="K -> N (in Ref. 2; AAA65602)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..123
FT /note="RAR -> PRT (in Ref. 2; AAA65602)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="E -> V (in Ref. 2; AAA65602)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="V -> G (in Ref. 2; AAA65602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 58208 MW; A76804E613F6893D CRC64;
MANEVISGEQ LQKVIRDAAD LVVSSAGVTL GPEGRPVIMS KSYGGPEVTK DGYKVINNLK
PEDEKIAKIV ELLNQATSQA NEKAGDGTTT ATILVGNMIK NAHKHIAAQR SRTKLKSGMK
RARDEVVKYI QSVAKKINSE EEIAQVGSIS ANGNSEIGNK IAEAMNKVGK EGVITVEEGK
GLDEFSVSVV QGMVFDRGYV SPYFITNPEK MIVEFDNPYV LLANKKLSSI QPMVPLLETI
VRSNRAVVII AEDVEGEALT SLVLSKMRGS LKACAVKAPG FGDRRSEMLE DIRILTGAKT
LVSDDLGVTV ESLTVEDLGT AKSIIISKDS TTIVDGGGEK TSIDARVKQI KTQIDKTTSD
YDKEKLQERL AKLAGGVAVL KVGGATEVEV KERKDRVEDA LHATRAAVEE GIVPGGGATL
LSAIAVLEKL SSDDDDEQAG INIVKSALKA PISQIVENAG EDASVITYNL LESKDPNRIF
DARELKYVDA FKAGIIDPAK VVRVALESAV SVASVLVTTE ALIVDLPTKD NGSPSMMPGG
GMGGMGGF
