ID CH10_ECOLI Reviewed; 97 AA. AC P0A6F9; P05380; Q2M6G2; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580, ECO:0000305}; DE AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580, ECO:0000305}; DE AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580, ECO:0000303|PubMed:10532860}; DE Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580, ECO:0000303|PubMed:10532860}; GN Name=groES {ECO:0000255|HAMAP-Rule:MF_00580, GN ECO:0000303|PubMed:7015340}; Synonyms=groS, mopB; GN OrderedLocusNames=b4142, JW4102; 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 [GENOMIC DNA]. 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 [3] 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 [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-74. RX PubMed=7901771; DOI=10.1038/366279a0; RA Martin J., Geromanos S., Tempst P., Hartl F.U.; RT "Identification of nucleotide-binding regions in the chaperonin proteins RT GroEL and GroES."; RL Nature 366:279-282(1993). RN [7] RP PROTEIN SEQUENCE OF 1-18. RX PubMed=8506346; DOI=10.1073/pnas.90.11.5011; RA Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.; RT "Identifying proteins from two-dimensional gels by molecular mass searching RT of peptide fragments in protein sequence databases."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993). RN [8] RP PROTEIN SEQUENCE OF 1-11. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.; RL Submitted (SEP-1994) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 1-12. 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 [10] RP PROTEIN SEQUENCE OF 1-4. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726; RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., RA Hochstrasser D.F.; RT "Protein identification with N and C-terminal sequence tags in proteome RT projects."; RL J. Mol. Biol. 278:599-608(1998). 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 FUNCTION, SUBUNIT, AND INTERACTION WITH GROEL. 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 [17] RP SUBUNIT, AND INTERACTION WITH GROEL. 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 [18] RP SUBUNIT, AND INTERACTION WITH GROEL. 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 [19] RP SUBUNIT, AND INTERACTION WITH GROEL. 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 [20] RP SUBUNIT, AND INTERACTION WITH GROEL. 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 [21] 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 [22] RP FUNCTION. 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 [23] RP FUNCTION. 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 [24] 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 [25] 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 [26] RP SUCCINYLATION AT LYS-34. 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 [27] 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 [28] 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 [29] 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 [30] 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 [31] 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 [32] 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 [33] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX PubMed=8538739; DOI=10.1038/379037a0; RA Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Deisenhofer J.; RT "The crystal structure of the GroES co-chaperonin at 2.8-A resolution."; RL Nature 379:37-45(1996). RN [34] {ECO:0007744|PDB:1AON} RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GROEL, FUNCTION, AND RP SUBUNIT. 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 [35] {ECO:0007744|PDB:1EGS} RP STRUCTURE BY NMR OF 19-27. RX PubMed=8876186; DOI=10.1073/pnas.93.21.11622; RA Landry S.J., Taher A., Georgopoulos C., van der Vies S.M.; RT "Interplay of structure and disorder in cochaperonin mobile loops."; RL Proc. Natl. Acad. Sci. U.S.A. 93:11622-11627(1996). RN [36] {ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9} RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH GROEL. 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 [37] {ECO:0007744|PDB:3ZPZ, ECO:0007744|PDB:3ZQ0, ECO:0007744|PDB:3ZQ1} RP STRUCTURE BY ELECTRON MICROSCOPY (8.90 ANGSTROMS) IN COMPLEX WITH GROEL. 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 [38] {ECO:0007744|PDB:3WVL} RP X-RAY CRYSTALLOGRAPHY (3.79 ANGSTROMS) IN COMPLEX WITH GROEL, AND 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 [39] {ECO:0007744|PDB:5OPX} RP X-RAY CRYSTALLOGRAPHY (3.64 ANGSTROMS) IN COMPLEX WITH GROEL. 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 the chaperonin GroEL, plays an essential role CC in assisting protein folding (PubMed:2897629, PubMed:2573517, CC PubMed:10532860, PubMed:1676490, PubMed:16751100, PubMed:18418386, CC PubMed:18987317, PubMed:20603018, PubMed:24816391). The GroEL-GroES CC system forms a nano-cage that allows encapsulation of the non-native CC substrate proteins and provides a physical environment optimized to CC promote and accelerate protein folding, probably by preventing CC aggregation and by entropically destabilizing folding intermediates CC (PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, CC PubMed:24816391). GroES binds to the apical surface of the GroEL ring, CC thereby capping the opening of the GroEL channel (PubMed:9285585). CC Regulates the ATPase activity of GroEL (PubMed:1676490, CC PubMed:1361169). {ECO:0000269|PubMed:10532860, CC ECO:0000269|PubMed:1361169, ECO:0000269|PubMed:16751100, CC ECO:0000269|PubMed:1676490, ECO:0000269|PubMed:18418386, CC ECO:0000269|PubMed:18987317, ECO:0000269|PubMed:20603018, CC ECO:0000269|PubMed:24816391, ECO:0000269|PubMed:2573517, CC ECO:0000269|PubMed:2897629, ECO:0000269|PubMed:9285585}. CC -!- FUNCTION: (Microbial infection) Essential for the assembly of several CC bacteriophages. {ECO:0000269|PubMed:379350, CC ECO:0000269|PubMed:7015340}. CC -!- ACTIVITY REGULATION: Activity of the GroEL-GroES chaperonin complex CC requires Mg-ATP. {ECO:0000269|PubMed:10532860}. CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring (PubMed:1361169, CC PubMed:9285585). Interacts with the chaperonin GroEL (PubMed:1361169, CC PubMed:7638600, PubMed:7638601, PubMed:8618836, PubMed:8663256, CC PubMed:9285585, PubMed:25174333). Can form asymmetrical complexes, CC composed of one GroEL and one GroES, and symmetrical complexes, formed CC between one GroEL and two GroES oligomers (PubMed:1361169, CC PubMed:7638600, PubMed:7638601, PubMed:8618836, PubMed:8663256, CC PubMed:25174333). The asymmetrical complex is the functional unit CC (PubMed:7638600, PubMed:7638601, PubMed:25912285). It was suggested CC that the symmetric heterooligomer may represent a transient CC intermediate in the chaperonin protein folding cycle (PubMed:8618836, CC PubMed:8663256). Another study shows that the symmetric heterooligomers CC are substantially populated only in the presence of proteins that CC cannot be folded by the chaperonin (PubMed:25912285). CC {ECO:0000269|PubMed:1361169, ECO:0000269|PubMed:25174333, CC ECO:0000269|PubMed:25912285, ECO:0000269|PubMed:7638600, CC ECO:0000269|PubMed:7638601, ECO:0000269|PubMed:8618836, CC ECO:0000269|PubMed:8663256, ECO:0000269|PubMed:9285585}. CC -!- INTERACTION: CC P0A6F9; P0A6F5: groEL; NbExp=31; IntAct=EBI-369169, EBI-543750; CC P0A6F9; P0A6F9: groES; NbExp=2; IntAct=EBI-369169, EBI-369169; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580, CC ECO:0000269|PubMed:22380631}. Note=Exclusively localized in foci, CC usually near 1 cell pole in mid-to-late exponential phase; polar CC localization depends on the minCDE operon. Foci form near midcell. CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP- CC Rule:MF_00580, 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; CAA30697.1; -; Genomic_DNA. DR EMBL; X07899; CAA30738.1; -; Genomic_DNA. DR EMBL; U14003; AAA97041.1; -; Genomic_DNA. DR EMBL; U00096; AAC77102.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78144.1; -; Genomic_DNA. DR PIR; S03931; BVECGS. DR RefSeq; NP_418566.1; NC_000913.3. DR RefSeq; WP_001026276.1; NZ_STEB01000014.1. DR PDB; 1AON; X-ray; 3.00 A; O/P/Q/R/S/T/U=1-97. DR PDB; 1EGS; NMR; -; A=19-27. DR PDB; 1GRU; EM; 12.50 A; O/P/Q/R/S/T/U=1-97. DR PDB; 1PCQ; X-ray; 2.81 A; O/P/Q/R/S/T/U=1-97. DR PDB; 1PF9; X-ray; 2.99 A; O/P/Q/R/S/T/U=1-97. DR PDB; 1SVT; X-ray; 2.81 A; O/P/Q/R/S/T/U=1-97. DR PDB; 1SX4; X-ray; 3.00 A; O/P/Q/R/S/T/U=1-97. DR PDB; 2C7C; EM; 7.70 A; O/P/Q/R/S/T/U=1-97. DR PDB; 2C7D; EM; 8.70 A; O/P/Q/R/S/T/U=1-97. DR PDB; 3WVL; X-ray; 3.79 A; O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-97. DR PDB; 3ZPZ; EM; 8.90 A; O/P/Q/R/S/T/U=1-97. DR PDB; 3ZQ0; EM; 9.20 A; O/P/Q/R/S/T/U=1-97. DR PDB; 3ZQ1; EM; 15.90 A; O/P/Q/R/S/T/U=1-97. DR PDB; 5OPX; X-ray; 3.64 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-97. DR PDB; 7PBJ; EM; 3.40 A; Af/Am/At/Ba/Bh/Bo/Bv=1-97. DR PDB; 7PBX; EM; 3.43 A; Af/Al/Ar/Ax/Bd/Bj/Bp=1-97. DR PDB; 7VWX; EM; 7.60 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-97. DR PDB; 8BKZ; EM; 2.30 A; AA/B/CA/D/F/H/J/L/N/P/R/T/W/Y=2-97. DR PDB; 8BM0; EM; 3.40 A; B/E/J/M/P/S/W=2-97. DR PDB; 8BM1; EM; 2.70 A; B/E/J/M/P/S/W=2-97. DR PDB; 8BMO; EM; 3.40 A; D/G/K/N/Q/T/W=2-97. DR PDB; 8BMT; EM; 2.50 A; AA/B/CA/D/F/H/K/M/O/Q/S/V/W/Y=2-97. DR PDBsum; 1AON; -. DR PDBsum; 1EGS; -. DR PDBsum; 1GRU; -. DR PDBsum; 1PCQ; -. DR PDBsum; 1PF9; -. DR PDBsum; 1SVT; -. DR PDBsum; 1SX4; -. DR PDBsum; 2C7C; -. DR PDBsum; 2C7D; -. DR PDBsum; 3WVL; -. DR PDBsum; 3ZPZ; -. DR PDBsum; 3ZQ0; -. DR PDBsum; 3ZQ1; -. DR PDBsum; 5OPX; -. DR PDBsum; 7PBJ; -. DR PDBsum; 7PBX; -. DR PDBsum; 7VWX; -. DR PDBsum; 8BKZ; -. DR PDBsum; 8BM0; -. DR PDBsum; 8BM1; -. DR PDBsum; 8BMO; -. DR PDBsum; 8BMT; -. DR AlphaFoldDB; P0A6F9; -. DR EMDB; EMD-1046; -. DR EMDB; EMD-1180; -. DR EMDB; EMD-1181; -. DR EMDB; EMD-13293; -. DR EMDB; EMD-13308; -. DR EMDB; EMD-16099; -. DR EMDB; EMD-16116; -. DR EMDB; EMD-16117; -. 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 SMR; P0A6F9; -. DR BioGRID; 4262198; 222. DR ComplexPortal; CPX-2113; GroEL-GroES complex. DR DIP; DIP-9835N; -. DR IntAct; P0A6F9; 41. DR MINT; P0A6F9; -. DR STRING; 511145.b4142; -. DR jPOST; P0A6F9; -. DR PaxDb; 511145-b4142; -. DR EnsemblBacteria; AAC77102; AAC77102; b4142. DR GeneID; 83579149; -. DR GeneID; 948655; -. DR KEGG; ecj:JW4102; -. DR KEGG; eco:b4142; -. DR PATRIC; fig|1411691.4.peg.2558; -. DR EchoBASE; EB0595; -. DR eggNOG; COG0234; Bacteria. DR HOGENOM; CLU_132825_1_1_6; -. DR InParanoid; P0A6F9; -. DR OMA; EDFLIMR; -. DR OrthoDB; 9806791at2; -. DR PhylomeDB; P0A6F9; -. DR BioCyc; EcoCyc:EG10600-MONOMER; -. DR BioCyc; MetaCyc:EG10600-MONOMER; -. DR SABIO-RK; P0A6F9; -. DR EvolutionaryTrace; P0A6F9; -. DR PRO; PR:P0A6F9; -. 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:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0044183; F:protein folding chaperone; IEA:InterPro. DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:EcoCyc. DR GO; GO:0006457; P:protein folding; IDA:CACAO. DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki. DR GO; GO:0019068; P:virion assembly; IMP:EcoliWiki. DR CDD; cd00320; cpn10; 1. DR Gene3D; 2.30.33.40; GroES chaperonin; 1. DR HAMAP; MF_00580; CH10; 1. DR InterPro; IPR020818; Chaperonin_GroES. DR InterPro; IPR037124; Chaperonin_GroES_sf. DR InterPro; IPR018369; Chaprnonin_Cpn10_CS. DR InterPro; IPR011032; GroES-like_sf. DR PANTHER; PTHR10772; 10 KDA HEAT SHOCK PROTEIN; 1. DR PANTHER; PTHR10772:SF0; 10 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR PROSITE; PS00681; CHAPERONINS_CPN10; 1. DR SWISS-2DPAGE; P0A6F9; -. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; KW Reference proteome. FT CHAIN 1..97 FT /note="Co-chaperonin GroES" FT /id="PRO_0000174746" FT MOD_RES 34 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT CONFLICT 89 FT /note="S -> N (in Ref. 2; CAA30738)" FT /evidence="ECO:0000305" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:8BM1" FT STRAND 9..14 FT /evidence="ECO:0007829|PDB:8BM1" FT TURN 20..23 FT /evidence="ECO:0007829|PDB:1PCQ" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:8BM1" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:8BM1" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:1PCQ" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:1PCQ" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:8BM1" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:8BM0" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:8BM1" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:8BM1" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:8BM1" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:8BM1" SQ SEQUENCE 97 AA; 10387 MW; 76829E09B11217EF CRC64; MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA //