CH10_ECOLI
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 03-AUG-2022, entry version 152.
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, ECO:0000303|PubMed:7015340};
GN Synonyms=groS, mopB; OrderedLocusNames=b4142, JW4102;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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}.
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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 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 AlphaFoldDB; P0A6F9; -.
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 SWISS-2DPAGE; P0A6F9; -.
DR jPOST; P0A6F9; -.
DR PaxDb; P0A6F9; -.
DR PRIDE; P0A6F9; -.
DR EnsemblBacteria; AAC77102; AAC77102; b4142.
DR EnsemblBacteria; BAE78144; BAE78144; BAE78144.
DR GeneID; 67414760; -.
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; RSINMTI; -.
DR PhylomeDB; P0A6F9; -.
DR BioCyc; EcoCyc:EG10600-MON; -.
DR BioCyc; MetaCyc:EG10600-MON; -.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion 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; -; 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; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
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 2..5
FT /evidence="ECO:0007829|PDB:1PCQ"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:1PCQ"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1PCQ"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1PCQ"
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:1PCQ"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1PCQ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1PCQ"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1PCQ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1PCQ"
SQ SEQUENCE 97 AA; 10387 MW; 76829E09B11217EF CRC64;
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK
VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA
