ID   CH60_COXBU              Reviewed;         552 AA.
AC   P19421;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 133.
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}, htpB, mopA;
GN   OrderedLocusNames=CBU_1718;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3343219; DOI=10.1128/jb.170.3.1227-1234.1988;
RA   Vodkin M.H., Williams J.C.;
RT   "A heat shock operon in Coxiella burnetti produces a major antigen
RT   homologous to a protein in both mycobacteria and Escherichia coli.";
RL   J. Bacteriol. 170:1227-1234(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Nine Mile Crazy / RSA 514;
RX   PubMed=17088354; DOI=10.1128/iai.00883-06;
RA   Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J.,
RA   Samuel J.E., Heinzen R.A.;
RT   "Proteome and antigen profiling of Coxiella burnetii developmental forms.";
RL   Infect. Immun. 75:290-298(2007).
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   -!- DEVELOPMENTAL STAGE: Present in large cell variant (LCV) stage and
CC       small cell variant (SCV) stage (at protein level). LCVs are more
CC       metabolically active than SCVs. {ECO:0000269|PubMed:17088354}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR   EMBL; M20482; AAA23309.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO91213.1; -; Genomic_DNA.
DR   PIR; S39765; S39765.
DR   RefSeq; NP_820699.1; NC_002971.3.
DR   RefSeq; WP_005770500.1; NZ_CDBG01000001.1.
DR   AlphaFoldDB; P19421; -.
DR   SMR; P19421; -.
DR   STRING; 227377.CBU_1718; -.
DR   EnsemblBacteria; AAO91213; AAO91213; CBU_1718.
DR   GeneID; 1209629; -.
DR   KEGG; cbu:CBU_1718; -.
DR   PATRIC; fig|227377.7.peg.1703; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_6; -.
DR   OMA; TDTDKME; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
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; Isomerase; Nucleotide-binding;
KW   Reference proteome; Stress response.
FT   CHAIN           1..552
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063354"
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         480..482
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         496
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   552 AA;  58284 MW;  D248857BDB6B1B5E CRC64;
     MAAKVLKFSH EVLHAMSRGV EVLANAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAKEI
     ELEDKFENMG AQMVKEVASR TSDDAGDGTT TATVLAQAIL VEGIKAVIAG MNPMDLKRGI
     DKAVTAAVAE LKKISKPCKD QKAIAQVGTI SANSDKSIGD IIAEAMEKVG KEGVITVEDG
     SGLENALEVV EGMQFDRGYL SPYFINNQQN MSAELENPFI LLVDKKISNI RELIPLLENV
     AKSGRPLLVI AEDIEGEALA TLVVNNIRGV VKVAAVKAPG FGDRRKAMLQ DIAVLTGGKV
     ISEEVGLSLE AASLDDLGSA KRVVVTKDDT TIIDGSGDAG DIKNRVEQIR KEIENSSSDY
     DKEKLQERLA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVPGGGVALI
     RVLKSLDSVE VENEDQRVGV EIARRAMAYP LSQIVKNTGV QAAVVADKVL NHKDVNYGYN
     AATGEYGDMI EMGILDPTKV TRTALQNAAS IAGLMITTEC MVTEAPKKKE ESMPGGGDMG
     GMGGMGGMGG MM