Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P0A6F5 (CH60_ECOLI)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    60 kDa chaperonin
Alternative name(s):
    Protein Cpn60
    groEL protein
Gene names
Name: groL
Synonyms: groEL, mopA
Ordered Locus Names: b4143, JW4103
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. HAMAP MF_00600

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. HAMAP MF_00600

Subunit structure

Oligomer of 14 subunits composed of two stacked rings of 7 subunits. HAMAP MF_00600

Subcellular location

Cytoplasm. HAMAP MF_00600

Post-translational modification

Phosphorylated reversibly during heat shock. Ref.10

Miscellaneous

This protein shows ATPase activity. HAMAP MF_00600

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Caution

Was originally (Ref.6) designated as the ams protein.

Sequence caution

The sequence AAA23934.1 differs from that shown. Reason: Frameshift at positions 424 and 455.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-543750,EBI-543750
aceEP0AFG81EBI-543750,EBI-542683
adiYP332341EBI-543750,EBI-1119007
alsAP327211EBI-543750,EBI-562166
astBP762161EBI-543750,EBI-1125311
astCP775811EBI-543750,EBI-1125336
atoDP764581EBI-543750,EBI-555870
chbRP174101EBI-543750,EBI-1125285
choP762131EBI-543750,EBI-545155
cofP468911EBI-543750,EBI-1117256
cysHP178541EBI-543750,EBI-1114555
dapEP0AED71EBI-543750,EBI-1129009
dnaNP0A9881EBI-543750,EBI-542385
dusBP0ABT51EBI-543750,EBI-1124821
dusCP333711EBI-543750,EBI-562765
epdP0A9B61EBI-543750,EBI-1130931
eutBP0AEJ61EBI-543750,EBI-1128853
eutGP765531EBI-543750,EBI-1128863
fecEP150311EBI-543750,EBI-1132949
fhlAP193231EBI-543750,EBI-1113147
frvRP321521EBI-543750,EBI-1133981
gcvAP0A9F61EBI-543750,EBI-1130436
glgAP0A6U81EBI-543750,EBI-1132777
groSP0A6F93EBI-543750,EBI-369169
gspAP457561EBI-543750,EBI-1132428
hcaEP0ABR51EBI-543750,EBI-1115311
hisHP605951EBI-543750,EBI-1126953
hisPP071091EBI-543750,EBI-1120883
hldDP679101EBI-543750,EBI-543760
holAP286301EBI-543750,EBI-549153
hydNP0AAK41EBI-543750,EBI-1130039
hyfGP773292EBI-543750,EBI-548413
idnRP393431EBI-543750,EBI-1133947
lsrAP772571EBI-543750,EBI-1124301
mazGP0AEY31EBI-543750,EBI-554166
metAP076231EBI-543750,EBI-1134411
modCP098331EBI-543750,EBI-1120112
mtlAP005501EBI-543750,EBI-547239
nhaRP0A9G21EBI-543750,EBI-1112817
phnCP166771EBI-543750,EBI-1134635
phnLP166791EBI-543750,EBI-1125776
phpP455481EBI-543750,EBI-1123441
potAP698741EBI-543750,EBI-1122336
pphAP557981EBI-543750,EBI-1125727
proSP166591EBI-543750,EBI-549550
prpRP777431EBI-543750,EBI-1115838
prsP0A7171EBI-543750,EBI-906827
purCP0A7D71EBI-543750,EBI-555481
purUP370511EBI-543750,EBI-1122931
rbsRP0ACQ01EBI-543750,EBI-1119646
recFP0A7H01EBI-543750,EBI-556839
rfaQP257421EBI-543750,EBI-555525
rfbCP377451EBI-543750,EBI-557071
rimJP0A9481EBI-543750,EBI-1115189
rmlA2P618871EBI-543750,EBI-550893
rndP091551EBI-543750,EBI-1125527
rspAP381041EBI-543750,EBI-1115648
rssAP0AFR01EBI-543750,EBI-1122950
ruvCP0A8141EBI-543750,EBI-1123014
sdhBP070141EBI-543750,EBI-1035514
sgbHP376781EBI-543750,EBI-555448
sgcQP393641EBI-543750,EBI-1135119
sgcRP393611EBI-543750,EBI-1135102
sppAP083951EBI-543750,EBI-909838
thiHP301401EBI-543750,EBI-1125553
ttcAP760551EBI-543750,EBI-1123658
ttdBP0AC351EBI-543750,EBI-1129625
tyrBP046931EBI-543750,EBI-1114498
ulaEP393051EBI-543750,EBI-1134968
ulaRP0A9W01EBI-543750,EBI-560926
uspGP391771EBI-543750,EBI-561722
vacJP765061EBI-543750,EBI-1128511
yaaAP0A8I31EBI-543750,EBI-559258
yafMQ471521EBI-543750,EBI-1114849
yagAP370071EBI-543750,EBI-556783
ybbLP772791EBI-543750,EBI-560090
ybfFP757361EBI-543750,EBI-1119842
ycbJP0AB031EBI-543750,EBI-1120953
ycjSP775031EBI-543750,EBI-1123489
ydcRP777301EBI-543750,EBI-549487
ydeMP761341EBI-543750,EBI-1124264
ydfHP0ACM21EBI-543750,EBI-1124452
ydiFP377661EBI-543750,EBI-1125110
ydiUP776491EBI-543750,EBI-1125166
yeaUP762511EBI-543750,EBI-560661
yecEP373481EBI-543750,EBI-1125864
yedLP763191EBI-543750,EBI-1126470
yehHP333451EBI-543750,EBI-1114721
yfaXP777321EBI-543750,EBI-549004
yfbHP764721EBI-543750,EBI-1128209
yfjNP521291EBI-543750,EBI-560462
ygaEP373381EBI-543750,EBI-1120314
ygaFP373391EBI-543750,EBI-555990
ygbMQ468911EBI-543750,EBI-1130107
ygdHP0ADR81EBI-543750,EBI-549313
ygeAP038131EBI-543750,EBI-545190
ygeHP766391EBI-543750,EBI-1130602
ygfJQ468101EBI-543750,EBI-1121055
yggRP520521EBI-543750,EBI-552531
yghTQ468441EBI-543750,EBI-1120199
yghZQ468511EBI-543750,EBI-1131219
yhbUP455271EBI-543750,EBI-561157
yhcMP646121EBI-543750,EBI-1132081
yhdZP457691EBI-543750,EBI-1127595
yhiLP376291EBI-543750,EBI-1130402
yhjBP376401EBI-543750,EBI-542016
yhjHP376461EBI-543750,EBI-1122546
yicIP314341EBI-543750,EBI-1122922
yidPP314531EBI-543750,EBI-1133529
yidZP314631EBI-543750,EBI-556561
yihRP321391EBI-543750,EBI-553107
yjeSP392881EBI-543750,EBI-1133090
yjfZP393081EBI-543750,EBI-551424
yjgZP393511EBI-543750,EBI-1125297
yjhPP393671EBI-543750,EBI-1135127
yjiCP393741EBI-543750,EBI-1135135
yjiEP393761EBI-543750,EBI-1131228
yjiRP393891EBI-543750,EBI-1113411
ypdBP0AE391EBI-543750,EBI-1128681
ypdCP773961EBI-543750,EBI-1128701
ypdFP765241EBI-543750,EBI-1128711
yrbFP633861EBI-543750,EBI-561408
ytfMP0ADE41EBI-543750,EBI-1114298

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 54854760 kDa chaperonin HAMAP MF_00600
PRO_0000063358

Amino acid modifications

Modified residue1171N6-acetyllysine Ref.12

Experimental info

Sequence conflict83 – 864DAAG → GALQ in CAA30739. Ref.5
Sequence conflict2621L → A in CAA30698. Ref.1
Sequence conflict2671M → I in CAA30698. Ref.1
Sequence conflict3431Q → R in AAA23934. Ref.6

Secondary structure

1 ................................................................................... 548
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P0A6F5-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CD3A0FB505F74AD1

FASTA54857,329
        10         20         30         40         50         60 
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI 

        70         80         90        100        110        120 
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI 

       130        140        150        160        170        180 
DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG 

       190        200        210        220        230        240 
TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV 

       250        260        270        280        290        300 
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 

       310        320        330        340        350        360 
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY 

       370        380        390        400        410        420 
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI 

       430        440        450        460        470        480 
RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA 

       490        500        510        520        530        540 
ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG 


MGGMGGMM

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Homologous plant and bacterial proteins chaperone oligomeric protein assembly."
Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., Georgopoulos C., Hendrix R.W., Ellis R.J.
Nature 333:330-334(1988) [PubMed: 2897629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Control of cell division by sex factor F in Escherichia coli. III. Participation of the groES (mopB) gene of the host bacteria."
Miki T., Orita T., Furuno M., Horiuchi T.
J. Mol. Biol. 201:327-338(1988) [PubMed: 2901493] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
[6]"Cloning, sequence analysis, and expression of alteration of the mRNA stability gene (ams+) of Escherichia coli."
Chanda P.K., Ono M., Kuwano M., Kung H.-F.
J. Bacteriol. 161:446-449(1985) [PubMed: 2578448] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-495.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22.
Strain: K12 / EMG2.
[8]Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
Submitted (FEB-1996) to UniProtKB
Cited for: PARTIAL PROTEIN SEQUENCE OF 2-12.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]"The reaction of GroEL (cpn 60) with the ATP analogue 2',3' dialdehyde ATP."
Thomson G.J., Coggins J.R., Price N.C.
FEBS Lett. 336:19-22(1993) [PubMed: 7903255] [Abstract]
Cited for: PROTEIN SEQUENCE OF 455-519.
[10]"Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation."
Sherman M.Y., Goldberg A.L.
Nature 357:167-169(1992) [PubMed: 1349729] [Abstract]
Cited for: PHOSPHORYLATION.
[11]"Residues in chaperonin GroEL required for polypeptide binding and release."
Fenton W.A., Kashi Y., Furtak K., Horwich A.L.
Nature 371:614-619(1994) [PubMed: 7935796] [Abstract]
Cited for: MUTAGENESIS.
[12]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, MASS SPECTROMETRY.
[13]"The crystal structure of the bacterial chaperonin GroEL at 2.8 A."
Braig K., Otwinowski Z., Hegde R.S., Boisvert D.C., Joachimiak A., Horwich A.L., Sigler P.B.
Nature 371:578-586(1994) [PubMed: 7935790] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[14]"Conformational variability in the refined structure of the chaperonin GroEL at 2.8-A resolution."
Braig K., Adams P.D., Bruenger A.T.
Nat. Struct. Biol. 2:1083-1094(1995) [PubMed: 8846220] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[15]"The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S."
Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B.
Nat. Struct. Biol. 3:170-177(1996) [PubMed: 8564544] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[16]"Chaperone activity and structure of monomeric polypeptide binding domains of GroEL."
Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., Fersht A.R.
Proc. Natl. Acad. Sci. U.S.A. 93:15024-15029(1996) [PubMed: 8986757] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[17]"The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex."
Xu Z., Horwich A.L., Sigler P.B.
Nature 388:741-750(1997) [PubMed: 9285585] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[18]"The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity."
Chen L., Sigler P.B.
Cell 99:757-768(1999) [PubMed: 10619429] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 192-337.
[19]"Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions."
Kiser P.D., Lodowski D.T., Palczewski K.
Acta Crystallogr. F 63:457-461(2007) [PubMed: 17554162] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS).

Hide | Top

Cross-references

Sequence databases

X07850 Genomic DNA. Translation: CAA30698.1.
U14003 Genomic DNA. Translation: AAA97042.1.
U00096 Genomic DNA. Translation: AAC77103.1.
AP009048 Genomic DNA. Translation: BAE78145.1.
X07899 Genomic DNA. Translation: CAA30739.1.
M11294 Genomic DNA. Translation: AAA23934.1. Frameshift.
PIRBVECGL. S56371.
RefSeqAP_004644.1.
NP_418567.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AONX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1DK7X-ray2.02A/B191-336[»]
1DKDX-ray2.10A/B/C/D191-336[»]
1FY9X-ray2.20A191-376[»]
1FYAX-ray2.20A191-376[»]
1GR5electron microscopy7.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1GRLX-ray2.80A/B/C/D/E/F/G1-548[»]
1GRUelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1J4ZX-ray3.52A/B/C/D/E/F/G/H/I/J/K/L/M/N2-547[»]
1JONX-ray2.50A191-345[»]
1KIDX-ray1.70A191-375[»]
1KP8X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-547[»]
1KPOX-ray3.521/2/O/P/Q/R/S/T/U/V/W/X/Y/Z2-547[»]
1LA1X-ray2.06A188-379[»]
1MNFX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-547[»]
1OELX-ray2.80A/B/C/D/E/F/G2-548[»]
1PCQX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-524[»]
1PF9X-ray2.99A/B/C/D/E/F/G/H/I/J/K/L/M/N1-525[»]
1SS8X-ray2.70A/B/C/D/E/F/G2-524[»]
1SVTX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-524[»]
1SX3X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1SX4X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-524[»]
1XCKX-ray2.92A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
2C7Celectron microscopy7.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-547[»]
2C7Delectron microscopy8.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-547[»]
2C7Eelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2CGTelectron microscopy8.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-547[»]
2EU1X-ray3.29A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
2NWCX-ray3.02A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
3C9Velectron microscopy4.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3CAUelectron microscopy4.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:339N.
IntActP0A6F5. 688 interactions.

2-D gel databases

SWISS-2DPAGEP0A6F5.
2DBase-EcoliP0A6F5.
ECO2DBASEB056.5. 6TH EDITION.

Genome annotation databases

GeneID948665.
GenomeReviewsGene locus JW4103 in contig AP009048_GR.
Gene locus b4143 in contig U00096_GR.
KEGGecj:JW4103.
eco:b4143.

Organism-specific databases

EchoBASEEB0594.
EcoGeneEG10599. groL.
CMRSearch...

Phylogenomic databases

HOGENOMP0A6F5.
OMAP0A6F5. TANAGDE.

Enzyme and pathway databases

BioCycEcoCyc:EG10599-MON.

Family and domain databases

HAMAPMF_00600.
[Tree]
InterProIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
[Graphical view]
PANTHERPTHR11353. Cpn60/TCP-1. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00298. CHAPERONIN60.
TIGRFAMsTIGR02348. GroEL. 1 hit.
PROSITEPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCH60_ECOLI
AccessionPrimary (citable) accession number: P0A6F5
Secondary accession number(s): P06139, Q2M6G1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents