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60 kDa chaperonin (GroEL protein) (Protein Cpn60)

 CH60_ECOLI              Reviewed;         548 AA.
P0A6F5; P06139; Q2M6G1;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 136.
RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600};
AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
Name=groL {ECO:0000255|HAMAP-Rule:MF_00600};
Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
OrderedLocusNames=b4143, JW4103;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2897629; DOI=10.1038/333330a0;
Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K.,
Dennis D.T., Georgopoulos C., Hendrix R.W., Ellis R.J.;
"Homologous plant and bacterial proteins chaperone oligomeric protein
assembly.";
Nature 333:330-334(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the
region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
PubMed=2901493; DOI=10.1016/0022-2836(88)90141-6;
Miki T., Orita T., Furuno M., Horiuchi T.;
"Control of cell division by sex factor F in Escherichia coli. III.
Participation of the groES (mopB) gene of the host bacteria.";
J. Mol. Biol. 201:327-338(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-495.
PubMed=2578448;
Chanda P.K., Ono M., Kuwano M., Kung H.-F.;
"Cloning, sequence analysis, and expression of alteration of the mRNA
stability gene (ams+) of Escherichia coli.";
J. Bacteriol. 161:446-449(1985).
[7]
PROTEIN SEQUENCE OF 2-22.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
PROTEIN SEQUENCE OF 2-12.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
Submitted (FEB-1996) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 4-10.
STRAIN=K12;
PubMed=17895580; DOI=10.1266/ggs.82.291;
Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
"A role of RnlA in the RNase LS activity from Escherichia coli.";
Genes Genet. Syst. 82:291-299(2007).
[10]
PROTEIN SEQUENCE OF 455-519.
PubMed=7903255; DOI=10.1016/0014-5793(93)81600-5;
Thomson G.J., Coggins J.R., Price N.C.;
"The reaction of GroEL (cpn 60) with the ATP analogue 2',3' dialdehyde
ATP.";
FEBS Lett. 336:19-22(1993).
[11]
PHOSPHORYLATION.
PubMed=1349729; DOI=10.1038/357167a0;
Sherman M.Y., Goldberg A.L.;
"Heat shock in Escherichia coli alters the protein-binding properties
of the chaperonin groEL by inducing its phosphorylation.";
Nature 357:167-169(1992).
[12]
MUTAGENESIS.
PubMed=7935796; DOI=10.1038/371614a0;
Fenton W.A., Kashi Y., Furtak K., Horwich A.L.;
"Residues in chaperonin GroEL required for polypeptide binding and
release.";
Nature 371:614-619(1994).
[13]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[14]
SUBUNIT, AND MUTAGENESIS OF ALA-2 AND GLU-76.
PubMed=15327959; DOI=10.1016/j.jmb.2004.07.066;
Qamra R., Srinivas V., Mande S.C.;
"Mycobacterium tuberculosis GroEL homologues unusually exist as lower
oligomers and retain the ability to suppress aggregation of substrate
proteins.";
J. Mol. Biol. 342:605-617(2004).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[16]
SUBCELLULAR LOCATION.
PubMed=20094032; DOI=10.1038/emboj.2009.412;
Winkler J., Seybert A., Konig L., Pruggnaller S., Haselmann U.,
Sourjik V., Weiss M., Frangakis A.S., Mogk A., Bukau B.;
"Quantitative and spatio-temporal features of protein aggregation in
Escherichia coli and consequences on protein quality control and
cellular ageing.";
EMBO J. 29:910-923(2010).
[17]
SUCCINYLATION AT LYS-34; LYS-51; LYS-117; LYS-277; LYS-321 AND
LYS-390.
STRAIN=K12;
PubMed=21151122; DOI=10.1038/nchembio.495;
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
"Identification of lysine succinylation as a new post-translational
modification.";
Nat. Chem. Biol. 7:58-63(2011).
[18]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
Li G., Young K.D.;
"Isolation and identification of new inner membrane-associated
proteins that localize to cell poles in Escherichia coli.";
Mol. Microbiol. 84:276-295(2012).
[19]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=7935790; DOI=10.1038/371578a0;
Braig K., Otwinowski Z., Hegde R.S., Boisvert D.C., Joachimiak A.,
Horwich A.L., Sigler P.B.;
"The crystal structure of the bacterial chaperonin GroEL at 2.8 A.";
Nature 371:578-586(1994).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=8846220; DOI=10.1038/nsb1295-1083;
Braig K., Adams P.D., Bruenger A.T.;
"Conformational variability in the refined structure of the chaperonin
GroEL at 2.8-A resolution.";
Nat. Struct. Biol. 2:1083-1094(1995).
[21]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=8564544; DOI=10.1038/nsb0296-170;
Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B.;
"The 2.4 A crystal structure of the bacterial chaperonin GroEL
complexed with ATP gamma S.";
Nat. Struct. Biol. 3:170-177(1996).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8986757; DOI=10.1073/pnas.93.26.15024;
Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J.,
Golbik R., Fersht A.R.;
"Chaperone activity and structure of monomeric polypeptide binding
domains of GroEL.";
Proc. Natl. Acad. Sci. U.S.A. 93:15024-15029(1996).
[23]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=9285585; DOI=10.1038/41944;
Xu Z., Horwich A.L., Sigler P.B.;
"The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin
complex.";
Nature 388:741-750(1997).
[24]
X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 192-337.
PubMed=10619429; DOI=10.1016/S0092-8674(00)81673-6;
Chen L., Sigler P.B.;
"The crystal structure of a GroEL/peptide complex: plasticity as a
basis for substrate diversity.";
Cell 99:757-768(1999).
[25]
X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS).
PubMed=17554162; DOI=10.1107/S1744309107020295;
Kiser P.D., Lodowski D.T., Palczewski K.;
"Purification, crystallization and structure determination of native
GroEL from Escherichia coli lacking bound potassium ions.";
Acta Crystallogr. F 63:457-461(2007).
-!- FUNCTION: Prevents misfolding and promotes the refolding and
proper assembly of unfolded polypeptides generated under stress
conditions.
-!- FUNCTION: Essential for the growth of the bacteria and the
assembly of several bacteriophages. Also plays a role in coupling
between replication of the F plasmid and cell division of the
cell.
-!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of
7 subunits. Complex can be destablized when Ala-2 and Glu-76 are
mutated to match these residues in M.tuberculosis
(PubMed:15327959). {ECO:0000269|PubMed:15327959}.
-!- INTERACTION:
Self; NbExp=11; IntAct=EBI-543750, EBI-543750;
P0AFG8:aceE; NbExp=3; IntAct=EBI-543750, EBI-542683;
P60010:ACT1 (xeno); NbExp=5; IntAct=EBI-543750, EBI-2169;
P00887:aroH; NbExp=3; IntAct=EBI-543750, EBI-1125143;
P76213:cho; NbExp=3; IntAct=EBI-543750, EBI-545155;
P77279:fetA; NbExp=3; IntAct=EBI-543750, EBI-560090;
P19323:fhlA; NbExp=2; IntAct=EBI-543750, EBI-1113147;
P0A6F9:groS; NbExp=31; IntAct=EBI-543750, EBI-369169;
P09372:grpE; NbExp=3; IntAct=EBI-543750, EBI-547441;
P77329:hyfG; NbExp=4; IntAct=EBI-543750, EBI-548413;
P0AEX9:malE; NbExp=3; IntAct=EBI-543750, EBI-369910;
P0AEY3:mazG; NbExp=2; IntAct=EBI-543750, EBI-554166;
P0A817:metK; NbExp=2; IntAct=EBI-543750, EBI-546295;
P63386:mlaF; NbExp=4; IntAct=EBI-543750, EBI-561408;
P13423:pagA (xeno); NbExp=2; IntAct=EBI-543750, EBI-456868;
P0A717:prs; NbExp=2; IntAct=EBI-543750, EBI-906827;
P0A7H0:recF; NbExp=4; IntAct=EBI-543750, EBI-556839;
P37745:rfbC; NbExp=3; IntAct=EBI-543750, EBI-557071;
P0AGB3:rpoH; NbExp=3; IntAct=EBI-543750, EBI-555342;
P00586:TST (xeno); NbExp=2; IntAct=EBI-543750, EBI-7900146;
P0A9W0:ulaR; NbExp=4; IntAct=EBI-543750, EBI-560926;
P39177:uspG; NbExp=5; IntAct=EBI-543750, EBI-561722;
P45527:yhbU; NbExp=4; IntAct=EBI-543750, EBI-561157;
P37640:yhjB; NbExp=3; IntAct=EBI-543750, EBI-542016;
P76524:ypdF; NbExp=2; IntAct=EBI-543750, EBI-1128711;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600,
ECO:0000269|PubMed:20094032, ECO:0000269|PubMed:22380631}.
Note=Uniformly located in the cytoplasm (PubMed:20094032).
Exclusively localized in foci, usually near 1 cell pole in mid-to-
late exponential phase (PubMed:22380631); polar localization
depends on the minCDE operon. Foci form near midcell (Probable).
{ECO:0000269|PubMed:20094032, ECO:0000269|PubMed:22380631,
ECO:0000305}.
-!- PTM: Phosphorylated reversibly during heat shock.
{ECO:0000269|PubMed:1349729}.
-!- MISCELLANEOUS: This protein shows ATPase activity.
-!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
{ECO:0000255|HAMAP-Rule:MF_00600}.
-!- CAUTION: Was originally designated as the ams protein.
{ECO:0000305|PubMed:2578448}.
-!- SEQUENCE CAUTION:
Sequence=AAA23934.1; Type=Frameshift; Positions=424, 455; Evidence={ECO:0000305};
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EMBL; X07850; CAA30698.1; -; Genomic_DNA.
EMBL; U14003; AAA97042.1; -; Genomic_DNA.
EMBL; U00096; AAC77103.1; -; Genomic_DNA.
EMBL; AP009048; BAE78145.1; -; Genomic_DNA.
EMBL; X07899; CAA30739.1; -; Genomic_DNA.
EMBL; M11294; AAA23934.1; ALT_FRAME; Genomic_DNA.
PIR; S56371; BVECGL.
RefSeq; NP_418567.1; NC_000913.3.
RefSeq; WP_000729117.1; NZ_LN832404.1.
PDB; 1AON; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 1DK7; X-ray; 2.02 A; A/B=191-336.
PDB; 1DKD; X-ray; 2.10 A; A/B/C/D=191-336.
PDB; 1FY9; X-ray; 2.20 A; A=191-376.
PDB; 1FYA; X-ray; 2.20 A; A=191-376.
PDB; 1GR5; EM; 7.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 1GRL; X-ray; 2.80 A; A/B/C/D/E/F/G=1-548.
PDB; 1GRU; EM; 12.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 1JON; X-ray; 2.50 A; A=191-345.
PDB; 1KID; X-ray; 1.70 A; A=188-376.
PDB; 1KP8; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 1LA1; X-ray; 2.06 A; A=188-379.
PDB; 1MNF; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 1OEL; X-ray; 2.80 A; A/B/C/D/E/F/G=2-548.
PDB; 1PCQ; X-ray; 2.81 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525.
PDB; 1PF9; X-ray; 2.99 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525.
PDB; 1SS8; X-ray; 2.70 A; A/B/C/D/E/F/G=2-525.
PDB; 1SVT; X-ray; 2.81 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525.
PDB; 1SX3; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-526.
PDB; 1SX4; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525.
PDB; 1XCK; X-ray; 2.92 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 2C7C; EM; 7.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 2C7D; EM; 8.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 2C7E; EM; 9.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 2CGT; EM; 8.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 2EU1; X-ray; 3.29 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 2NWC; X-ray; 3.02 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548.
PDB; 2YEY; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525.
PDB; 3C9V; EM; 4.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527.
PDB; 3CAU; EM; 4.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527.
PDB; 3VZ6; X-ray; 1.50 A; A=191-376.
PDB; 3VZ7; X-ray; 1.80 A; A=191-376.
PDB; 3VZ8; X-ray; 1.90 A; A/B/C=191-376.
PDB; 3WVL; X-ray; 3.79 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 3ZPZ; EM; 8.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527.
PDB; 3ZQ0; EM; 9.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525.
PDB; 3ZQ1; EM; 15.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-527.
PDB; 4AAQ; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 4AAR; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 4AAS; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 4AAU; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 4AB2; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 4AB3; EM; 8.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
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.
PDB; 4WGL; X-ray; 3.13 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDB; 4WSC; X-ray; 3.04 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-548.
PDBsum; 1AON; -.
PDBsum; 1DK7; -.
PDBsum; 1DKD; -.
PDBsum; 1FY9; -.
PDBsum; 1FYA; -.
PDBsum; 1GR5; -.
PDBsum; 1GRL; -.
PDBsum; 1GRU; -.
PDBsum; 1JON; -.
PDBsum; 1KID; -.
PDBsum; 1KP8; -.
PDBsum; 1LA1; -.
PDBsum; 1MNF; -.
PDBsum; 1OEL; -.
PDBsum; 1PCQ; -.
PDBsum; 1PF9; -.
PDBsum; 1SS8; -.
PDBsum; 1SVT; -.
PDBsum; 1SX3; -.
PDBsum; 1SX4; -.
PDBsum; 1XCK; -.
PDBsum; 2C7C; -.
PDBsum; 2C7D; -.
PDBsum; 2C7E; -.
PDBsum; 2CGT; -.
PDBsum; 2EU1; -.
PDBsum; 2NWC; -.
PDBsum; 2YEY; -.
PDBsum; 3C9V; -.
PDBsum; 3CAU; -.
PDBsum; 3VZ6; -.
PDBsum; 3VZ7; -.
PDBsum; 3VZ8; -.
PDBsum; 3WVL; -.
PDBsum; 3ZPZ; -.
PDBsum; 3ZQ0; -.
PDBsum; 3ZQ1; -.
PDBsum; 4AAQ; -.
PDBsum; 4AAR; -.
PDBsum; 4AAS; -.
PDBsum; 4AAU; -.
PDBsum; 4AB2; -.
PDBsum; 4AB3; -.
PDBsum; 4V43; -.
PDBsum; 4WGL; -.
PDBsum; 4WSC; -.
ProteinModelPortal; P0A6F5; -.
SMR; P0A6F5; -.
BioGrid; 4263077; 558.
BioGrid; 852957; 1.
DIP; DIP-339N; -.
IntAct; P0A6F5; 700.
MINT; MINT-5232496; -.
STRING; 316385.ECDH10B_4336; -.
iPTMnet; P0A6F5; -.
SWISS-2DPAGE; P0A6F5; -.
PaxDb; P0A6F5; -.
PRIDE; P0A6F5; -.
EnsemblBacteria; AAC77103; AAC77103; b4143.
EnsemblBacteria; BAE78145; BAE78145; BAE78145.
GeneID; 948665; -.
KEGG; ecj:JW4103; -.
KEGG; eco:b4143; -.
PATRIC; fig|1411691.4.peg.2557; -.
EchoBASE; EB0594; -.
EcoGene; EG10599; groL.
eggNOG; ENOG4105CJ9; Bacteria.
eggNOG; COG0459; LUCA.
HOGENOM; HOG000076290; -.
InParanoid; P0A6F5; -.
KO; K04077; -.
PhylomeDB; P0A6F5; -.
BioCyc; EcoCyc:EG10599-MONOMER; -.
BioCyc; MetaCyc:EG10599-MONOMER; -.
BRENDA; 3.6.4.9; 2026.
SABIO-RK; P0A6F5; -.
EvolutionaryTrace; P0A6F5; -.
PRO; PR:P0A6F5; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:1990220; C:GroEL-GroES complex; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
GO; GO:0016887; F:ATPase activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0044183; F:protein binding involved in protein folding; IBA:GO_Central.
GO; GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:EcoCyc.
GO; GO:0006457; P:protein folding; IMP:EcoCyc.
GO; GO:0042026; P:protein refolding; IEA:InterPro.
GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
GO; GO:0019068; P:virion assembly; IMP:EcoliWiki.
CDD; cd03344; GroEL; 1.
Gene3D; 1.10.560.10; -; 2.
Gene3D; 3.50.7.10; -; 1.
HAMAP; MF_00600; CH60; 1.
InterPro; IPR018370; Chaperonin_Cpn60_CS.
InterPro; IPR001844; Chaprnin_Cpn60.
InterPro; IPR002423; Cpn60/TCP-1.
InterPro; IPR037290; Cpn60/TCP-1_sf.
InterPro; IPR027409; GroEL-like_apical_dom_sf.
InterPro; IPR027413; GROEL-like_equatorial_sf.
PANTHER; PTHR11353; PTHR11353; 1.
Pfam; PF00118; Cpn60_TCP1; 1.
PRINTS; PR00298; CHAPERONIN60.
SUPFAM; SSF48592; SSF48592; 2.
SUPFAM; SSF52029; SSF52029; 1.
SUPFAM; SSF54849; SSF54849; 1.
TIGRFAMs; TIGR02348; GroEL; 1.
PROSITE; PS00296; CHAPERONINS_CPN60; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing;
Nucleotide-binding; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298646,
ECO:0000269|Ref.8}.
CHAIN 2 548 60 kDa chaperonin.
/FTId=PRO_0000063358.
MOD_RES 34 34 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 51 51 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 117 117 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18723842}.
MOD_RES 117 117 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:21151122}.
MOD_RES 277 277 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 321 321 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 390 390 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MUTAGEN 2 2 A->S: Complex stability is significantly
decreased; when associated with S-76,
same residues as in M.tuberculosis.
{ECO:0000269|PubMed:15327959}.
MUTAGEN 76 76 E->S: Complex stability is significantly
decreased; when associated with S-2, same
residues as in M.tuberculosis.
{ECO:0000269|PubMed:15327959}.
CONFLICT 83 86 DAAG -> GALQ (in Ref. 5; CAA30739).
{ECO:0000305}.
CONFLICT 262 262 L -> A (in Ref. 1; CAA30698).
{ECO:0000305}.
CONFLICT 267 267 M -> I (in Ref. 1; CAA30698).
{ECO:0000305}.
CONFLICT 343 343 Q -> R (in Ref. 6; AAA23934).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:1KP8}.
HELIX 9 28 {ECO:0000244|PDB:1KP8}.
STRAND 37 40 {ECO:0000244|PDB:1KP8}.
STRAND 43 46 {ECO:0000244|PDB:1KP8}.
STRAND 48 50 {ECO:0000244|PDB:1KP8}.
HELIX 53 59 {ECO:0000244|PDB:1KP8}.
HELIX 65 85 {ECO:0000244|PDB:1KP8}.
HELIX 89 108 {ECO:0000244|PDB:1KP8}.
HELIX 113 134 {ECO:0000244|PDB:1KP8}.
HELIX 141 151 {ECO:0000244|PDB:1KP8}.
TURN 152 154 {ECO:0000244|PDB:1SS8}.
HELIX 156 169 {ECO:0000244|PDB:1KP8}.
STRAND 173 178 {ECO:0000244|PDB:1KP8}.
STRAND 181 184 {ECO:0000244|PDB:1KP8}.
STRAND 186 191 {ECO:0000244|PDB:1KP8}.
STRAND 193 196 {ECO:0000244|PDB:3VZ6}.
STRAND 199 201 {ECO:0000244|PDB:1KP8}.
HELIX 202 204 {ECO:0000244|PDB:3VZ6}.
TURN 208 211 {ECO:0000244|PDB:3VZ6}.
STRAND 212 217 {ECO:0000244|PDB:3VZ6}.
STRAND 219 227 {ECO:0000244|PDB:3VZ6}.
HELIX 230 233 {ECO:0000244|PDB:3VZ6}.
HELIX 234 243 {ECO:0000244|PDB:3VZ6}.
STRAND 247 254 {ECO:0000244|PDB:3VZ6}.
HELIX 256 267 {ECO:0000244|PDB:3VZ6}.
STRAND 268 270 {ECO:0000244|PDB:1OEL}.
STRAND 273 277 {ECO:0000244|PDB:3VZ6}.
STRAND 279 281 {ECO:0000244|PDB:3VZ6}.
HELIX 282 296 {ECO:0000244|PDB:3VZ6}.
STRAND 300 302 {ECO:0000244|PDB:1XCK}.
HELIX 303 305 {ECO:0000244|PDB:3VZ6}.
HELIX 309 311 {ECO:0000244|PDB:3VZ6}.
HELIX 314 316 {ECO:0000244|PDB:3VZ6}.
STRAND 317 325 {ECO:0000244|PDB:3VZ6}.
STRAND 330 335 {ECO:0000244|PDB:3VZ6}.
HELIX 339 355 {ECO:0000244|PDB:3VZ6}.
HELIX 359 375 {ECO:0000244|PDB:3VZ6}.
STRAND 376 380 {ECO:0000244|PDB:1KP8}.
HELIX 386 409 {ECO:0000244|PDB:1KP8}.
STRAND 411 413 {ECO:0000244|PDB:1KP8}.
TURN 414 416 {ECO:0000244|PDB:1KP8}.
HELIX 417 425 {ECO:0000244|PDB:1KP8}.
TURN 426 428 {ECO:0000244|PDB:1KP8}.
HELIX 434 446 {ECO:0000244|PDB:1KP8}.
HELIX 449 457 {ECO:0000244|PDB:1KP8}.
HELIX 462 471 {ECO:0000244|PDB:1KP8}.
STRAND 476 479 {ECO:0000244|PDB:1KP8}.
TURN 480 483 {ECO:0000244|PDB:1KP8}.
STRAND 484 487 {ECO:0000244|PDB:1KP8}.
TURN 488 492 {ECO:0000244|PDB:1KP8}.
STRAND 494 496 {ECO:0000244|PDB:1KP8}.
HELIX 497 515 {ECO:0000244|PDB:1KP8}.
STRAND 517 523 {ECO:0000244|PDB:1KP8}.
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


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