ID CH60_ECOLI Reviewed; 548 AA. AC P0A6F5; P06139; Q2M6G1; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000305}; DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:9285585, ECO:0000269|PubMed:9285593}; DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000303|PubMed:10532860}; DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000303|PubMed:10532860}; DE AltName: Full=GroEL protein {ECO:0000305}; GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600, GN ECO:0000303|PubMed:7015340}; GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA; GN OrderedLocusNames=b4143, JW4103; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=2897629; DOI=10.1038/333330a0; RA Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., RA Georgopoulos C., Hendrix R.W., Ellis R.J.; RT "Homologous plant and bacterial proteins chaperone oligomeric protein RT assembly."; RL Nature 333:330-334(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86, AND FUNCTION. RX PubMed=2901493; DOI=10.1016/0022-2836(88)90141-6; RA Miki T., Orita T., Furuno M., Horiuchi T.; RT "Control of cell division by sex factor F in Escherichia coli. III. RT Participation of the groES (mopB) gene of the host bacteria."; RL J. Mol. Biol. 201:327-338(1988). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-495. RX PubMed=2578448; DOI=10.1128/jb.161.1.446-449.1985; RA Chanda P.K., Ono M., Kuwano M., Kung H.-F.; RT "Cloning, sequence analysis, and expression of alteration of the mRNA RT stability gene (ams+) of Escherichia coli."; RL J. Bacteriol. 161:446-449(1985). RN [7] RP PROTEIN SEQUENCE OF 2-22. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [8] RP PROTEIN SEQUENCE OF 2-12. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.; RL Submitted (FEB-1996) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 4-10. RC STRAIN=K12; RX PubMed=17895580; DOI=10.1266/ggs.82.291; RA Otsuka Y., Koga M., Iwamoto A., Yonesaki T.; RT "A role of RnlA in the RNase LS activity from Escherichia coli."; RL Genes Genet. Syst. 82:291-299(2007). RN [10] RP PROTEIN SEQUENCE OF 455-519. RX PubMed=7903255; DOI=10.1016/0014-5793(93)81600-5; RA Thomson G.J., Coggins J.R., Price N.C.; RT "The reaction of GroEL (cpn 60) with the ATP analogue 2',3' dialdehyde RT ATP."; RL FEBS Lett. 336:19-22(1993). RN [11] RP FUNTION (MICROBIAL INFECTION). RX PubMed=379350; DOI=10.1016/0022-2836(79)90502-3; RA Hendrix R.W.; RT "Purification and properties of groE, a host protein involved in RT bacteriophage assembly."; RL J. Mol. Biol. 129:375-392(1979). RN [12] RP FUNTION (MICROBIAL INFECTION), AND GENE NAME. RX PubMed=7015340; DOI=10.1073/pnas.78.3.1629; RA Tilly K., Murialdo H., Georgopoulos C.; RT "Identification of a second Escherichia coli groE gene whose product is RT necessary for bacteriophage morphogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 78:1629-1633(1981). RN [13] RP FUNCTION. RX PubMed=2573517; DOI=10.1002/j.1460-2075.1989.tb08517.x; RA Kusukawa N., Yura T., Ueguchi C., Akiyama Y., Ito K.; RT "Effects of mutations in heat-shock genes groES and groEL on protein export RT in Escherichia coli."; RL EMBO J. 8:3517-3521(1989). RN [14] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=10532860; DOI=10.1038/342884a0; RA Goloubinoff P., Christeller J.T., Gatenby A.A., Lorimer G.H.; RT "Reconstitution of active dimeric ribulose bisphosphate carboxylase from an RT unfoleded state depends on two chaperonin proteins and Mg-ATP."; RL Nature 342:884-889(1989). RN [15] RP FUNCTION. RX PubMed=1676490; DOI=10.1038/352036a0; RA Martin J., Langer T., Boteva R., Schramel A., Horwich A.L., Hartl F.U.; RT "Chaperonin-mediated protein folding at the surface of groEL through a RT 'molten globule'-like intermediate."; RL Nature 352:36-42(1991). RN [16] RP PHOSPHORYLATION. RX PubMed=1349729; DOI=10.1038/357167a0; RA Sherman M.Y., Goldberg A.L.; RT "Heat shock in Escherichia coli alters the protein-binding properties of RT the chaperonin groEL by inducing its phosphorylation."; RL Nature 357:167-169(1992). RN [17] RP SUBUNIT, AND INTERACTION WITH GROES. RX PubMed=1361169; DOI=10.1002/j.1460-2075.1992.tb05581.x; RA Langer T., Pfeifer G., Martin J., Baumeister W., Hartl F.U.; RT "Chaperonin-mediated protein folding: GroES binds to one end of the GroEL RT cylinder, which accommodates the protein substrate within its central RT cavity."; RL EMBO J. 11:4757-4765(1992). RN [18] RP FUNCTION, AND MUTAGENESIS OF GLU-461. RX PubMed=8104102; DOI=10.1016/0092-8674(93)90470-b; RA Horwich A.L., Low K.B., Fenton W.A., Hirshfield I.N., Furtak K.; RT "Folding in vivo of bacterial cytoplasmic proteins: role of GroEL."; RL Cell 74:909-917(1993). RN [19] RP FUNCTION. RX PubMed=7915201; DOI=10.1016/0092-8674(94)90533-9; RA Weissman J.S., Kashi Y., Fenton W.A., Horwich A.L.; RT "GroEL-mediated protein folding proceeds by multiple rounds of binding and RT release of nonnative forms."; RL Cell 78:693-702(1994). RN [20] RP MUTAGENESIS. RX PubMed=7935796; DOI=10.1038/371614a0; RA Fenton W.A., Kashi Y., Furtak K., Horwich A.L.; RT "Residues in chaperonin GroEL required for polypeptide binding and RT release."; RL Nature 371:614-619(1994). RN [21] RP FUNCTION. RX PubMed=7867798; DOI=10.1016/0014-5793(95)00041-7; RA Taguchi H., Yoshida M.; RT "Chaperonin releases the substrate protein in a form with tendency to RT aggregate and ability to rebind to chaperonin."; RL FEBS Lett. 359:195-198(1995). RN [22] RP SUBUNIT, AND INTERACTION WITH GROES. RX PubMed=8618836; DOI=10.1073/pnas.92.26.12021; RA Azem A., Diamant S., Kessel M., Weiss C., Goloubinoff P.; RT "The protein-folding activity of chaperonins correlates with the symmetric RT GroEL14(GroES7)2 heterooligomer."; RL Proc. Natl. Acad. Sci. U.S.A. 92:12021-12025(1995). RN [23] RP SUBUNIT, AND INTERACTION WITH GROES. RX PubMed=7638600; DOI=10.1126/science.7638600; RA Engel A., Hayer-Hartl M.K., Goldie K.N., Pfeifer G., Hegerl R., Mueller S., RA da Silva A.C., Baumeister W., Hartl F.U.; RT "Functional significance of symmetrical versus asymmetrical GroEL-GroES RT chaperonin complexes."; RL Science 269:832-836(1995). RN [24] RP SUBUNIT, AND INTERACTION WITH GROES. RX PubMed=7638601; DOI=10.1126/science.7638601; RA Hayer-Hartl M.K., Martin J., Hartl F.U.; RT "Asymmetrical interaction of GroEL and GroES in the ATPase cycle of RT assisted protein folding."; RL Science 269:836-841(1995). RN [25] RP FUNCTION. RX PubMed=8861908; DOI=10.1016/s0092-8674(00)81342-2; RA Roseman A.M., Chen S., White H., Braig K., Saibil H.R.; RT "The chaperonin ATPase cycle: mechanism of allosteric switching and RT movements of substrate-binding domains in GroEL."; RL Cell 87:241-251(1996). RN [26] RP SUBUNIT, AND INTERACTION WITH GROES. RX PubMed=8663256; DOI=10.1074/jbc.271.27.16180; RA Toeroek Z., Vigh L., Goloubinoff P.; RT "Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers RT involved in protein release during the chaperonin cycle."; RL J. Biol. Chem. 271:16180-16186(1996). RN [27] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [28] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF RP ASP-398. RX PubMed=9285593; DOI=10.1038/42047; RA Rye H.S., Burston S.G., Fenton W.A., Beechem J.M., Xu Z., Sigler P.B., RA Horwich A.L.; RT "Distinct actions of cis and trans ATP within the double ring of the RT chaperonin GroEL."; RL Nature 388:792-798(1997). RN [29] RP SUBUNIT, AND MUTAGENESIS OF ALA-2 AND GLU-76. RX PubMed=15327959; DOI=10.1016/j.jmb.2004.07.066; RA Qamra R., Srinivas V., Mande S.C.; RT "Mycobacterium tuberculosis GroEL homologues unusually exist as lower RT oligomers and retain the ability to suppress aggregation of substrate RT proteins."; RL J. Mol. Biol. 342:605-617(2004). RN [30] RP FUNCTION, AND DOMAIN. RX PubMed=16751100; DOI=10.1016/j.cell.2006.04.027; RA Tang Y.C., Chang H.C., Roeben A., Wischnewski D., Wischnewski N., RA Kerner M.J., Hartl F.U., Hayer-Hartl M.; RT "Structural features of the GroEL-GroES nano-cage required for rapid RT folding of encapsulated protein."; RL Cell 125:903-914(2006). RN [31] RP FUNCTION. RX PubMed=16684774; DOI=10.1074/jbc.m601605200; RA Cliff M.J., Limpkin C., Cameron A., Burston S.G., Clarke A.R.; RT "Elucidation of steps in the capture of a protein substrate for efficient RT encapsulation by GroE."; RL J. Biol. Chem. 281:21266-21275(2006). RN [32] RP FUNCTION, AND DOMAIN. RX PubMed=18418386; DOI=10.1038/emboj.2008.77; RA Tang Y.C., Chang H.C., Chakraborty K., Hartl F.U., Hayer-Hartl M.; RT "Essential role of the chaperonin folding compartment in vivo."; RL EMBO J. 27:1458-1468(2008). RN [33] RP FUNCTION. RX PubMed=18987317; DOI=10.1073/pnas.0809794105; RA Apetri A.C., Horwich A.L.; RT "Chaperonin chamber accelerates protein folding through passive action of RT preventing aggregation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:17351-17355(2008). RN [34] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [35] RP FUNCTION. RX PubMed=19915138; DOI=10.1073/pnas.0911556106; RA Tyagi N.K., Fenton W.A., Horwich A.L.; RT "GroEL/GroES cycling: ATP binds to an open ring before substrate protein RT favoring protein binding and production of the native state."; RL Proc. Natl. Acad. Sci. U.S.A. 106:20264-20269(2009). RN [36] RP FUNCTION. RX PubMed=20603018; DOI=10.1016/j.cell.2010.05.027; RA Chakraborty K., Chatila M., Sinha J., Shi Q., Poschner B.C., Sikor M., RA Jiang G., Lamb D.C., Hartl F.U., Hayer-Hartl M.; RT "Chaperonin-catalyzed rescue of kinetically trapped states in protein RT folding."; RL Cell 142:112-122(2010). RN [37] RP SUBCELLULAR LOCATION. RX PubMed=20094032; DOI=10.1038/emboj.2009.412; RA Winkler J., Seybert A., Konig L., Pruggnaller S., Haselmann U., Sourjik V., RA Weiss M., Frangakis A.S., Mogk A., Bukau B.; RT "Quantitative and spatio-temporal features of protein aggregation in RT Escherichia coli and consequences on protein quality control and cellular RT ageing."; RL EMBO J. 29:910-923(2010). RN [38] RP SUCCINYLATION AT LYS-34; LYS-51; LYS-117; LYS-277; LYS-321 AND LYS-390. RC STRAIN=K12; RX PubMed=21151122; DOI=10.1038/nchembio.495; RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.; RT "Identification of lysine succinylation as a new post-translational RT modification."; RL Nat. Chem. Biol. 7:58-63(2011). RN [39] RP FUNCTION. RX PubMed=22445172; DOI=10.1016/j.cell.2012.02.047; RA Clare D.K., Vasishtan D., Stagg S., Quispe J., Farr G.W., Topf M., RA Horwich A.L., Saibil H.R.; RT "ATP-triggered conformational changes delineate substrate-binding and RT -folding mechanics of the GroEL chaperonin."; RL Cell 149:113-123(2012). RN [40] RP SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x; RA Li G., Young K.D.; RT "Isolation and identification of new inner membrane-associated proteins RT that localize to cell poles in Escherichia coli."; RL Mol. Microbiol. 84:276-295(2012). RN [41] RP FUNCTION. RX PubMed=24816391; DOI=10.1016/j.jmb.2014.04.018; RA Gupta A.J., Haldar S., Milicic G., Hartl F.U., Hayer-Hartl M.; RT "Active cage mechanism of chaperonin-assisted protein folding demonstrated RT at single-molecule level."; RL J. Mol. Biol. 426:2739-2754(2014). RN [42] RP SUBUNIT. RX PubMed=25912285; DOI=10.1016/j.jmb.2015.04.009; RA Haldar S., Gupta A.J., Yan X., Milicic G., Hartl F.U., Hayer-Hartl M.; RT "Chaperonin-assisted protein folding: relative population of asymmetric and RT symmetric GroEL:GroES complexes."; RL J. Mol. Biol. 427:2244-2255(2015). RN [43] RP REVIEW. RX PubMed=19638247; DOI=10.1017/s0033583509004764; RA Horwich A.L., Fenton W.A.; RT "Chaperonin-mediated protein folding: using a central cavity to kinetically RT assist polypeptide chain folding."; RL Q. Rev. Biophys. 42:83-116(2009). RN [44] RP REVIEW. RX PubMed=26422689; DOI=10.1016/j.tibs.2015.07.009; RA Hayer-Hartl M., Bracher A., Hartl F.U.; RT "The GroEL-GroES chaperonin machine: a nano-cage for protein folding."; RL Trends Biochem. Sci. 41:62-76(2016). RN [45] RP REVIEW. RX PubMed=32446288; DOI=10.1002/1873-3468.13844; RA Balchin D., Hayer-Hartl M., Hartl F.U.; RT "Recent advances in understanding catalysis of protein folding by molecular RT chaperones."; RL FEBS Lett. 594:2770-2781(2020). RN [46] {ECO:0007744|PDB:1GRL} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, AND DOMAIN. RX PubMed=7935790; DOI=10.1038/371578a0; RA Braig K., Otwinowski Z., Hegde R.S., Boisvert D.C., Joachimiak A., RA Horwich A.L., Sigler P.B.; RT "The crystal structure of the bacterial chaperonin GroEL at 2.8 A."; RL Nature 371:578-586(1994). RN [47] {ECO:0007744|PDB:1OEL} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-548, AND SUBUNIT. RX PubMed=8846220; DOI=10.1038/nsb1295-1083; RA Braig K., Adams P.D., Bruenger A.T.; RT "Conformational variability in the refined structure of the chaperonin RT GroEL at 2.8-A resolution."; RL Nat. Struct. Biol. 2:1083-1094(1995). RN [48] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=8564544; DOI=10.1038/nsb0296-170; RA Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B.; RT "The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed RT with ATP gamma S."; RL Nat. Struct. Biol. 3:170-177(1996). RN [49] {ECO:0007744|PDB:1JON} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 191-345. RX PubMed=8986757; DOI=10.1073/pnas.93.26.15024; RA Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., RA Fersht A.R.; RT "Chaperone activity and structure of monomeric polypeptide binding domains RT of GroEL."; RL Proc. Natl. Acad. Sci. U.S.A. 93:15024-15029(1996). RN [50] {ECO:0007744|PDB:1AON} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-548 IN COMPLEX WITH GROES AND RP ADP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DOMAIN. RX PubMed=9285585; DOI=10.1038/41944; RA Xu Z., Horwich A.L., Sigler P.B.; RT "The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin RT complex."; RL Nature 388:741-750(1997). RN [51] {ECO:0007744|PDB:1DK7, ECO:0007744|PDB:1DKD} RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 192-337. RX PubMed=10619429; DOI=10.1016/s0092-8674(00)81673-6; RA Chen L., Sigler P.B.; RT "The crystal structure of a GroEL/peptide complex: plasticity as a basis RT for substrate diversity."; RL Cell 99:757-768(1999). RN [52] {ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9} RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 2-525 IN COMPLEX WITH GROES AND RP ADP. RX PubMed=14517228; DOI=10.1093/emboj/cdg477; RA Chaudhry C., Farr G.W., Todd M.J., Rye H.S., Brunger A.T., Adams P.D., RA Horwich A.L., Sigler P.B.; RT "Role of the gamma-phosphate of ATP in triggering protein folding by GroEL- RT GroES: function, structure and energetics."; RL EMBO J. 22:4877-4887(2003). RN [53] {ECO:0007744|PDB:1XCK} RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 2-548, AND DOMAIN. RX PubMed=16288915; DOI=10.1016/j.jmb.2005.09.096; RA Bartolucci C., Lamba D., Grazulis S., Manakova E., Heumann H.; RT "Crystal structure of wild-type chaperonin GroEL."; RL J. Mol. Biol. 354:940-951(2005). RN [54] {ECO:0007744|PDB:2NWC} RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS). RX PubMed=17554162; DOI=10.1107/s1744309107020295; RA Kiser P.D., Lodowski D.T., Palczewski K.; RT "Purification, crystallization and structure determination of native GroEL RT from Escherichia coli lacking bound potassium ions."; RL Acta Crystallogr. F 63:457-461(2007). RN [55] {ECO:0007744|PDB:3ZPZ, ECO:0007744|PDB:3ZQ0, ECO:0007744|PDB:3ZQ1} RP STRUCTURE BY ELECTRON MICROSCOPY (8.90 ANGSTROMS) OF 2-527 IN COMPLEX WITH RP GROES. RX PubMed=23746846; DOI=10.1016/j.cell.2013.04.052; RA Chen D.H., Madan D., Weaver J., Lin Z., Schroder G.F., Chiu W., Rye H.S.; RT "Visualizing GroEL/ES in the act of encapsulating a folding protein."; RL Cell 153:1354-1365(2013). RN [56] {ECO:0007744|PDB:3WVL} RP X-RAY CRYSTALLOGRAPHY (3.79 ANGSTROMS) IN COMPLEX WITH GROES AND ATP, AND RP SUBUNIT. RX PubMed=25174333; DOI=10.1016/j.jmb.2014.08.017; RA Koike-Takeshita A., Arakawa T., Taguchi H., Shimamura T.; RT "Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 RT complex determined at 3.8A reveals rearrangement between two GroEL rings."; RL J. Mol. Biol. 426:3634-3641(2014). RN [57] {ECO:0007744|PDB:5W0S} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 2-525. RX PubMed=28710336; DOI=10.1073/pnas.1704725114; RA Roh S.H., Hryc C.F., Jeong H.H., Fei X., Jakana J., Lorimer G.H., Chiu W.; RT "Subunit conformational variation within individual GroEL oligomers RT resolved by Cryo-EM."; RL Proc. Natl. Acad. Sci. U.S.A. 114:8259-8264(2017). RN [58] {ECO:0007744|PDB:5OPW, ECO:0007744|PDB:5OPX} RP X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) OF 2-548 IN COMPLEX WITH GROES, RP ACTIVITY REGULATION, AND MUTAGENESIS OF ALA-109. RX PubMed=29336887; DOI=10.1016/j.cell.2017.12.010; RA Yan X., Shi Q., Bracher A., Milicic G., Singh A.K., Hartl F.U., RA Hayer-Hartl M.; RT "GroEL ring separation and exchange in the chaperonin reaction."; RL Cell 172:605-617.e11(2018). CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential CC role in assisting protein folding (PubMed:2897629, PubMed:2573517, CC PubMed:10532860, PubMed:1676490, PubMed:8104102, PubMed:9285593, CC PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, CC PubMed:24816391). The GroEL-GroES system forms a nano-cage that allows CC encapsulation of the non-native substrate proteins and provides a CC physical environment optimized to promote and accelerate protein CC folding, probably by preventing aggregation and by entropically CC destabilizing folding intermediates (PubMed:16751100, PubMed:18418386, CC PubMed:18987317, PubMed:20603018, PubMed:24816391). Rapid binding of CC ATP, followed by slower binding of the non-native substrate protein and CC GroES to the cis open ring of GroEL initiates productive folding of the CC non-native protein inside a highly stable GroEL-ATP-GroES complex CC (PubMed:9285593, PubMed:9285585, PubMed:19915138, PubMed:22445172). CC Binding of ATP and GroES induces conformational changes that result in CC the release of the substrate protein into a nano-cage compartment, CC within the GroEL central cavity, for folding in isolation CC (PubMed:8861908, PubMed:9285585, PubMed:16684774, PubMed:22445172). To CC discharge GroES and substrate protein, ATP hydrolysis in the cis ring CC is required to form a GroEL-ADP-GroES complex with decreased stability CC (PubMed:9285593). Finally, binding of ATP to the opposite trans ring of CC GroEL results in disassembly of the cis-ternary complex, which opens CC the cage and allows release of the folded protein (PubMed:9285593, CC PubMed:9285585). Proteins released in non-native form may be rapidly CC rebound by another GroEL complex until all of the initially bound CC polypeptide reaches native form (PubMed:7915201, PubMed:7867798). Can CC rescue kinetically trapped intermediates (PubMed:20603018). GroEL shows CC ATPase activity (PubMed:379350, PubMed:1676490, PubMed:9285593). ATP CC hydrolysis moves the reaction cycle forward but is not required for CC substrate folding (PubMed:9285593). {ECO:0000269|PubMed:10532860, CC ECO:0000269|PubMed:16684774, ECO:0000269|PubMed:16751100, CC ECO:0000269|PubMed:1676490, ECO:0000269|PubMed:18418386, CC ECO:0000269|PubMed:18987317, ECO:0000269|PubMed:19915138, CC ECO:0000269|PubMed:20603018, ECO:0000269|PubMed:22445172, CC ECO:0000269|PubMed:24816391, ECO:0000269|PubMed:2573517, CC ECO:0000269|PubMed:2897629, ECO:0000269|PubMed:379350, CC ECO:0000269|PubMed:7867798, ECO:0000269|PubMed:7915201, CC ECO:0000269|PubMed:8104102, ECO:0000269|PubMed:8861908, CC ECO:0000269|PubMed:9285585, ECO:0000269|PubMed:9285593}. CC -!- FUNCTION: Also plays a role in coupling between replication of the F CC plasmid and cell division of the cell. {ECO:0000269|PubMed:2901493}. CC -!- FUNCTION: (Microbial infection) Essential for the assembly of several CC bacteriophages. {ECO:0000269|PubMed:379350, CC ECO:0000269|PubMed:7015340}. 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, ECO:0000269|PubMed:9285585, CC ECO:0000269|PubMed:9285593}; CC -!- ACTIVITY REGULATION: During the substrate-folding cycle, the two GroEL CC rings separate for effective substrate binding and chaperonin activity. CC Ring separation is triggered by ATP binding to the trans ring of the CC asymmetric GroEL:GroES complex and avoids formation of functionally CC impaired symmetric GroEL:GroES2 complexes (PubMed:29336887). Activity CC of the GroEL-GroES chaperonin complex requires Mg-ATP (PubMed:10532860, CC PubMed:9285593). {ECO:0000269|PubMed:10532860, CC ECO:0000269|PubMed:29336887, ECO:0000269|PubMed:9285593}. CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric CC rings stacked back-to-back (PubMed:1361169, PubMed:15327959, CC PubMed:7935790, PubMed:8846220, PubMed:9285585). Interacts with the co- CC chaperonin GroES (PubMed:1361169, PubMed:7638600, PubMed:7638601, CC PubMed:8618836, PubMed:8663256, PubMed:9285585, PubMed:25174333). Can CC form asymmetrical complexes, composed of one GroEL and one GroES, and CC symmetrical complexes, formed between one GroEL and two GroES oligomers CC (PubMed:1361169, PubMed:7638600, PubMed:7638601, PubMed:8618836, CC PubMed:8663256, PubMed:25174333). The asymmetrical complex is the CC functional unit (PubMed:7638600, PubMed:7638601, PubMed:25912285). It CC was suggested that the symmetric heterooligomer may represent a CC transient intermediate in the chaperonin protein folding cycle CC (PubMed:8618836, PubMed:8663256). Another study shows that the CC symmetric heterooligomers are substantially populated only in the CC presence of proteins that cannot be folded by the chaperonin CC (PubMed:25912285). {ECO:0000269|PubMed:1361169, CC ECO:0000269|PubMed:15327959, ECO:0000269|PubMed:25174333, CC ECO:0000269|PubMed:25912285, ECO:0000269|PubMed:7638600, CC ECO:0000269|PubMed:7638601, ECO:0000269|PubMed:7935790, CC ECO:0000269|PubMed:8618836, ECO:0000269|PubMed:8663256, CC ECO:0000269|PubMed:8846220, ECO:0000269|PubMed:9285585}. CC -!- INTERACTION: CC P0A6F5; P0AFG8: aceE; NbExp=3; IntAct=EBI-543750, EBI-542683; CC P0A6F5; P00887: aroH; NbExp=3; IntAct=EBI-543750, EBI-1125143; CC P0A6F5; P76213: cho; NbExp=3; IntAct=EBI-543750, EBI-545155; CC P0A6F5; P77279: fetA; NbExp=3; IntAct=EBI-543750, EBI-560090; CC P0A6F5; P19323: fhlA; NbExp=2; IntAct=EBI-543750, EBI-1113147; CC P0A6F5; P0A6F5: groEL; NbExp=11; IntAct=EBI-543750, EBI-543750; CC P0A6F5; P0A6F9: groES; NbExp=31; IntAct=EBI-543750, EBI-369169; CC P0A6F5; P09372: grpE; NbExp=3; IntAct=EBI-543750, EBI-547441; CC P0A6F5; P77329: hyfG; NbExp=4; IntAct=EBI-543750, EBI-548413; CC P0A6F5; P0AEX9: malE; NbExp=3; IntAct=EBI-543750, EBI-369910; CC P0A6F5; P0AEY3: mazG; NbExp=2; IntAct=EBI-543750, EBI-554166; CC P0A6F5; P0A817: metK; NbExp=2; IntAct=EBI-543750, EBI-546295; CC P0A6F5; P63386: mlaF; NbExp=4; IntAct=EBI-543750, EBI-561408; CC P0A6F5; P0A717: prs; NbExp=2; IntAct=EBI-543750, EBI-906827; CC P0A6F5; P0A7H0: recF; NbExp=4; IntAct=EBI-543750, EBI-556839; CC P0A6F5; P37745: rfbC; NbExp=3; IntAct=EBI-543750, EBI-557071; CC P0A6F5; P0AGB3: rpoH; NbExp=3; IntAct=EBI-543750, EBI-555342; CC P0A6F5; P45527: ubiU; NbExp=4; IntAct=EBI-543750, EBI-561157; CC P0A6F5; P0A9W0: ulaR; NbExp=4; IntAct=EBI-543750, EBI-560926; CC P0A6F5; P39177: uspG; NbExp=5; IntAct=EBI-543750, EBI-561722; CC P0A6F5; P37640: yhjB; NbExp=3; IntAct=EBI-543750, EBI-542016; CC P0A6F5; P76524: ypdF; NbExp=2; IntAct=EBI-543750, EBI-1128711; CC P0A6F5; P60010: ACT1; Xeno; NbExp=5; IntAct=EBI-543750, EBI-2169; CC P0A6F5; P13423: pagA; Xeno; NbExp=2; IntAct=EBI-543750, EBI-456868; CC P0A6F5; P00586: TST; Xeno; NbExp=2; IntAct=EBI-543750, EBI-7900146; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600, CC ECO:0000269|PubMed:20094032, ECO:0000269|PubMed:22380631}. CC Note=Uniformly located in the cytoplasm (PubMed:20094032). Exclusively CC localized in foci, usually near 1 cell pole in mid-to-late exponential CC phase (PubMed:22380631); polar localization depends on the minCDE CC operon. Foci form near midcell (Probable). CC {ECO:0000269|PubMed:20094032, ECO:0000269|PubMed:22380631, CC ECO:0000305}. CC -!- DOMAIN: Each subunit is composed of an apical domain that binds non- CC folded proteins and GroES, an intermediate domain and an equatorial CC domain that binds ATP and is involved in inter-ring interactions CC (PubMed:7935790, PubMed:16288915). Forms a large central channel that CC appears to traverse the entire length of the cylinder with no CC obstruction (PubMed:7935790). The central channel of GroEL functions as CC two cavities, one in each ring, that are separated from each other by CC the crystallographically disordered 23-amino-acid C-terminal segments CC of the seven subunits (PubMed:9285585). The entry and exit of CC polypeptide seem to be restricted to the apical end of each ring CC (PubMed:9285585). {ECO:0000269|PubMed:16288915, CC ECO:0000269|PubMed:7935790, ECO:0000269|PubMed:9285585}. CC -!- DOMAIN: Modulating the volume of the GroEL central cavity affects CC folding speed in accordance with confinement theory. Small proteins CC fold more rapidly as the size of the cage is gradually reduced to a CC point where restriction in space slows folding dramatically. For larger CC proteins, either expanding or reducing cage volume decelerate folding CC (PubMed:16751100). A stepwise reduction in cage size results in a CC gradual loss of cell viability (PubMed:18418386). CC {ECO:0000269|PubMed:16751100, ECO:0000269|PubMed:18418386}. CC -!- PTM: Phosphorylated reversibly during heat shock. CC {ECO:0000269|PubMed:1349729}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- CAUTION: Was originally designated as the ams protein. CC {ECO:0000305|PubMed:2578448}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA23934.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X07850; CAA30698.1; -; Genomic_DNA. DR EMBL; U14003; AAA97042.1; -; Genomic_DNA. DR EMBL; U00096; AAC77103.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78145.1; -; Genomic_DNA. DR EMBL; X07899; CAA30739.1; -; Genomic_DNA. DR EMBL; M11294; AAA23934.1; ALT_FRAME; Genomic_DNA. DR PIR; S56371; BVECGL. DR RefSeq; NP_418567.1; NC_000913.3. DR RefSeq; WP_000729117.1; NZ_STEB01000014.1. DR PDB; 1AON; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 1DK7; X-ray; 2.02 A; A/B=191-336. DR PDB; 1DKD; X-ray; 2.10 A; A/B/C/D=191-336. DR PDB; 1FY9; X-ray; 2.20 A; A=191-376. DR PDB; 1FYA; X-ray; 2.20 A; A=191-376. DR PDB; 1GR5; EM; 7.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 1GRL; X-ray; 2.80 A; A/B/C/D/E/F/G=1-548. DR PDB; 1GRU; EM; 12.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 1JON; X-ray; 2.50 A; A=191-345. DR PDB; 1KID; X-ray; 1.70 A; A=188-376. DR PDB; 1KP8; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 1LA1; X-ray; 2.06 A; A=188-379. DR PDB; 1MNF; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 1OEL; X-ray; 2.80 A; A/B/C/D/E/F/G=2-548. DR PDB; 1PCQ; X-ray; 2.81 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 1PF9; X-ray; 2.99 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 1SS8; X-ray; 2.70 A; A/B/C/D/E/F/G=2-525. DR PDB; 1SVT; X-ray; 2.81 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 1SX3; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-526. DR PDB; 1SX4; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 1XCK; X-ray; 2.92 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 2C7C; EM; 7.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 2C7D; EM; 8.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 2C7E; EM; 9.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 2CGT; EM; 8.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 2EU1; X-ray; 3.29 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 2NWC; X-ray; 3.02 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 2YEY; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 3C9V; EM; 4.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527. DR PDB; 3CAU; EM; 4.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527. DR PDB; 3VZ6; X-ray; 1.50 A; A=191-376. DR PDB; 3VZ7; X-ray; 1.80 A; A=191-376. DR PDB; 3VZ8; X-ray; 1.90 A; A/B/C=191-376. DR PDB; 3WVL; X-ray; 3.79 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 3ZPZ; EM; 8.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527. DR PDB; 3ZQ0; EM; 9.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 3ZQ1; EM; 15.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527. DR PDB; 4AAQ; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 4AAR; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 4AAS; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 4AAU; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 4AB2; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 4AB3; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 4V43; X-ray; 3.52 A; 1/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=2-548. DR PDB; 4WGL; X-ray; 3.13 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 4WSC; X-ray; 3.04 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 5OPW; X-ray; 3.19 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 5OPX; X-ray; 3.64 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 5W0S; EM; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 7PBJ; EM; 3.40 A; Ad/Ae/Ak/Al/Ar/As/Ay/Az/Bf/Bg/Bm/Bn/Bt/Bu=2-525. DR PDB; 7PBX; EM; 3.43 A; Ac/Ad/Ai/Aj/Ao/Ap/Au/Av/Ba/Bb/Bg/Bh/Bm/Bn=2-525. DR PDB; 7VWX; EM; 7.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 7XOJ; EM; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 7XOK; EM; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 7XOL; EM; 3.26 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 7XOM; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 7XON; EM; 3.10 A; B=2-548. DR PDB; 7XOO; EM; 3.00 A; B=2-548. DR PDB; 7XOP; EM; 3.20 A; K=2-548. DR PDB; 7XOQ; EM; 3.30 A; K=2-548. DR PDB; 7XOR; EM; 3.30 A; K=2-548. DR PDB; 7XOS; EM; 3.20 A; K=2-548. DR PDB; 7YWY; EM; 3.40 A; G/H/I/J/K/L/S/T/U/V/W/X/Z/b=2-525. DR PDB; 8BA7; EM; 4.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDB; 8BKZ; EM; 2.30 A; A/BA/C/E/G/I/K/M/O/Q/S/V/X/Z=1-548. DR PDB; 8BL2; EM; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BL7; EM; 4.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BLC; EM; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BLD; EM; 4.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BLE; EM; 4.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BLF; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BLY; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BM0; EM; 3.40 A; A/C/D/F/G/H/I/K/L/N/O/Q/R/T=1-548. DR PDB; 8BM1; EM; 2.70 A; A/C/D/F/G/H/I/K/L/N/O/Q/R/T=1-548. DR PDB; 8BMD; EM; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548. DR PDB; 8BMO; EM; 3.40 A; A/B/C/E/F/H/I/J/L/M/O/P/R/S=1-548. DR PDB; 8BMT; EM; 2.50 A; A/BA/C/E/G/I/J/L/N/P/R/T/X/Z=1-548. DR PDBsum; 1AON; -. DR PDBsum; 1DK7; -. DR PDBsum; 1DKD; -. DR PDBsum; 1FY9; -. DR PDBsum; 1FYA; -. DR PDBsum; 1GR5; -. DR PDBsum; 1GRL; -. DR PDBsum; 1GRU; -. DR PDBsum; 1JON; -. DR PDBsum; 1KID; -. DR PDBsum; 1KP8; -. DR PDBsum; 1LA1; -. DR PDBsum; 1MNF; -. DR PDBsum; 1OEL; -. DR PDBsum; 1PCQ; -. DR PDBsum; 1PF9; -. DR PDBsum; 1SS8; -. DR PDBsum; 1SVT; -. DR PDBsum; 1SX3; -. DR PDBsum; 1SX4; -. DR PDBsum; 1XCK; -. DR PDBsum; 2C7C; -. DR PDBsum; 2C7D; -. DR PDBsum; 2C7E; -. DR PDBsum; 2CGT; -. DR PDBsum; 2EU1; -. DR PDBsum; 2NWC; -. DR PDBsum; 2YEY; -. DR PDBsum; 3C9V; -. DR PDBsum; 3CAU; -. DR PDBsum; 3VZ6; -. DR PDBsum; 3VZ7; -. DR PDBsum; 3VZ8; -. DR PDBsum; 3WVL; -. DR PDBsum; 3ZPZ; -. DR PDBsum; 3ZQ0; -. DR PDBsum; 3ZQ1; -. DR PDBsum; 4AAQ; -. DR PDBsum; 4AAR; -. DR PDBsum; 4AAS; -. DR PDBsum; 4AAU; -. DR PDBsum; 4AB2; -. DR PDBsum; 4AB3; -. DR PDBsum; 4V43; -. DR PDBsum; 4WGL; -. DR PDBsum; 4WSC; -. DR PDBsum; 5OPW; -. DR PDBsum; 5OPX; -. DR PDBsum; 5W0S; -. DR PDBsum; 7PBJ; -. DR PDBsum; 7PBX; -. DR PDBsum; 7VWX; -. DR PDBsum; 7XOJ; -. DR PDBsum; 7XOK; -. DR PDBsum; 7XOL; -. DR PDBsum; 7XOM; -. DR PDBsum; 7XON; -. DR PDBsum; 7XOO; -. DR PDBsum; 7XOP; -. DR PDBsum; 7XOQ; -. DR PDBsum; 7XOR; -. DR PDBsum; 7XOS; -. DR PDBsum; 7YWY; -. DR PDBsum; 8BA7; -. DR PDBsum; 8BKZ; -. DR PDBsum; 8BL2; -. DR PDBsum; 8BL7; -. DR PDBsum; 8BLC; -. DR PDBsum; 8BLD; -. DR PDBsum; 8BLE; -. DR PDBsum; 8BLF; -. DR PDBsum; 8BLY; -. DR PDBsum; 8BM0; -. DR PDBsum; 8BM1; -. DR PDBsum; 8BMD; -. DR PDBsum; 8BMO; -. DR PDBsum; 8BMT; -. DR AlphaFoldDB; P0A6F5; -. DR EMDB; EMD-1042; -. DR EMDB; EMD-1046; -. DR EMDB; EMD-1047; -. DR EMDB; EMD-1180; -. DR EMDB; EMD-1181; -. DR EMDB; EMD-1202; -. DR EMDB; EMD-13293; -. DR EMDB; EMD-13308; -. DR EMDB; EMD-13762; -. DR EMDB; EMD-15939; -. DR EMDB; EMD-16099; -. DR EMDB; EMD-16100; -. DR EMDB; EMD-16102; -. DR EMDB; EMD-16106; -. DR EMDB; EMD-16107; -. DR EMDB; EMD-16108; -. DR EMDB; EMD-16109; -. DR EMDB; EMD-16115; -. DR EMDB; EMD-16116; -. DR EMDB; EMD-16117; -. DR EMDB; EMD-16118; -. DR EMDB; EMD-16119; -. DR EMDB; EMD-16125; -. DR EMDB; EMD-2325; -. DR EMDB; EMD-2326; -. DR EMDB; EMD-2327; -. DR EMDB; EMD-32164; -. DR EMDB; EMD-3407; -. DR EMDB; EMD-3415; -. DR EMDB; EMD-5001; -. DR EMDB; EMD-5002; -. DR EMDB; EMD-8750; -. DR SMR; P0A6F5; -. DR BioGRID; 4263077; 558. DR BioGRID; 852957; 8. DR ComplexPortal; CPX-2113; GroEL-GroES complex. DR DIP; DIP-339N; -. DR IntAct; P0A6F5; 700. DR MINT; P0A6F5; -. DR STRING; 511145.b4143; -. DR ChEMBL; CHEMBL4296299; -. DR CarbonylDB; P0A6F5; -. DR iPTMnet; P0A6F5; -. DR MetOSite; P0A6F5; -. DR jPOST; P0A6F5; -. DR PaxDb; 511145-b4143; -. DR EnsemblBacteria; AAC77103; AAC77103; b4143. DR GeneID; 75203974; -. DR GeneID; 948665; -. DR KEGG; ecj:JW4103; -. DR KEGG; eco:b4143; -. DR PATRIC; fig|1411691.4.peg.2557; -. DR EchoBASE; EB0594; -. DR eggNOG; COG0459; Bacteria. DR HOGENOM; CLU_016503_3_0_6; -. DR InParanoid; P0A6F5; -. DR OMA; TDTDKME; -. DR OrthoDB; 9766614at2; -. DR PhylomeDB; P0A6F5; -. DR BioCyc; EcoCyc:EG10599-MONOMER; -. DR BioCyc; MetaCyc:EG10599-MONOMER; -. DR BRENDA; 5.6.1.7; 2026. DR SABIO-RK; P0A6F5; -. DR EvolutionaryTrace; P0A6F5; -. DR PRO; PR:P0A6F5; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:1990220; C:GroEL-GroES complex; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc. DR GO; GO:0051082; F:unfolded protein binding; IDA:EcoCyc. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:EcoCyc. DR GO; GO:0006457; P:protein folding; IMP:EcoCyc. DR GO; GO:0042026; P:protein refolding; IBA:GO_Central. DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki. DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc. DR GO; GO:0019068; P:virion assembly; IMP:EcoliWiki. DR CDD; cd03344; GroEL; 1. DR Gene3D; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 NCBIfam; TIGR02348; GroEL; 1. DR PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. DR SWISS-2DPAGE; P0A6F5; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm; KW Direct protein sequencing; Isomerase; Nucleotide-binding; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298646, ECO:0000269|Ref.8" FT CHAIN 2..548 FT /note="Chaperonin GroEL" FT /id="PRO_0000063358" FT BINDING 30..33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600, FT ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, FT ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, FT ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, FT ECO:0007744|PDB:3WVL" FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600, FT ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, FT ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, FT ECO:0007744|PDB:1PF9, ECO:0007744|PDB:3WVL" FT BINDING 87..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600, FT ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, FT ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, FT ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, FT ECO:0007744|PDB:3WVL" FT BINDING 415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600, FT ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, FT ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, FT ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, FT ECO:0007744|PDB:3WVL" FT BINDING 479..481 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600, FT ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, FT ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, FT ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, FT ECO:0007744|PDB:3WVL" FT BINDING 495 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600, FT ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, FT ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, FT ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, FT ECO:0007744|PDB:3WVL" FT MOD_RES 34 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 51 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 117 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 117 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 277 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 321 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 390 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MUTAGEN 2 FT /note="A->S: Complex stability is significantly decreased; FT when associated with S-76, same residues as in FT M.tuberculosis." FT /evidence="ECO:0000269|PubMed:15327959" FT MUTAGEN 76 FT /note="E->S: Complex stability is significantly decreased; FT when associated with S-2, same residues as in FT M.tuberculosis." FT /evidence="ECO:0000269|PubMed:15327959" FT MUTAGEN 109 FT /note="A->C: Forms inter-ring disulfide bonds. Prevents FT ring separation and leads to the formation of high amounts FT of symmetric GroEL:GroES2 complexes." FT /evidence="ECO:0000269|PubMed:29336887" FT MUTAGEN 398 FT /note="D->A: Can bind ATP with normal affinity, but is FT defective in ATPase activity. Binds non-native rhodanese, FT but cannot release the protein." FT /evidence="ECO:0000269|PubMed:9285593" FT MUTAGEN 461 FT /note="E->K: Temperature-sensitive lethal mutant. At FT nonpermissive temperature, the rate of general translation FT is reduced and a defined group of cytoplasmic proteins are FT translated but fail to reach native form." FT /evidence="ECO:0000269|PubMed:8104102" FT CONFLICT 83..86 FT /note="DAAG -> GALQ (in Ref. 5; CAA30739)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="L -> A (in Ref. 1; CAA30698)" FT /evidence="ECO:0000305" FT CONFLICT 267 FT /note="M -> I (in Ref. 1; CAA30698)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="Q -> R (in Ref. 6; AAA23934)" FT /evidence="ECO:0000305" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 9..28 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:7YWY" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 53..59 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 65..85 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 89..108 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 113..134 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 141..151 FT /evidence="ECO:0007829|PDB:1KP8" FT TURN 152..154 FT /evidence="ECO:0007829|PDB:1SS8" FT HELIX 156..169 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 186..191 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 202..204 FT /evidence="ECO:0007829|PDB:3VZ6" FT TURN 208..211 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 212..217 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 219..227 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 230..233 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 234..243 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 247..254 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 256..267 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:8BL2" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 282..296 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:1XCK" FT HELIX 303..305 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 317..325 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 330..335 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 339..355 FT /evidence="ECO:0007829|PDB:3VZ6" FT HELIX 359..375 FT /evidence="ECO:0007829|PDB:3VZ6" FT STRAND 376..380 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 386..409 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:1KP8" FT TURN 414..416 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 417..425 FT /evidence="ECO:0007829|PDB:1KP8" FT TURN 426..428 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 434..446 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 449..457 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 462..471 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 476..479 FT /evidence="ECO:0007829|PDB:1KP8" FT TURN 480..483 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:1KP8" FT TURN 488..492 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:1KP8" FT HELIX 497..515 FT /evidence="ECO:0007829|PDB:1KP8" FT STRAND 517..523 FT /evidence="ECO:0007829|PDB:1KP8" SQ SEQUENCE 548 AA; 57329 MW; CD3A0FB505F74AD1 CRC64; MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM //