※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60 kDa chaperonin
Protein Synonyms/Alias
 
Gene Name
 groL
Gene Synonyms/Alias
 groEL, mopA; OrderedLocusNames=b4143, JW4103
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
154 VGTISANSDETVGKL S HTP [1]
157 ISANSDETVGKLIAE T HTP [1]
141 LSVPCSDSKAIAQVG S HTP [1]
55 TITKDGVSVAREIEL S HTP [1]
43 RNVVLDKSFGAPTIT S HTP [1]
360 IEEATSDYDREKLQE Y HTP [2]
Reference
 [1]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium.
 Soares NC,Spät P,Krug K,Macek B
 J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [PMID:23590516]
 [2]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence.
 Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A
 PLoS Pathog. 2013;9(6):e1003403. [PMID:23785281]
Functional Description From UniProt
 FUNCTION: Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions
Sequence Annotation From UniProt
 MOD_RES 34 34 N6-succinyllysine
 MOD_RES 51 51 N6-succinyllysine
 MOD_RES 117 117 N6-acetyllysine; alternate
 MOD_RES 117 117 N6-succinyllysine; alternate
 MOD_RES 277 277 N6-succinyllysine
 MOD_RES 321 321 N6-succinyllysine
 MOD_RES 390 390 N6-succinyllysine
Key Word From UniProt
 3D-structure; Acetylation; ATP-binding; Cellcycle; Celldivision; Chaperone; Completeproteome; Cytoplasm; Directproteinsequencing; Nucleotide-binding; Phosphoprotein; Referenceproteome
Protein Sequence
 MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI 60
 ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI 120
 DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG 180
 TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV 240
 AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 300
 ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY 360
 DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI 420
 RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA 480
 ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG 540
 MGGMGGMM 548
  GO:0005829   C:cytosol IDA:UniProtKB
  GO:0016020   C:membrane IDA:UniProtKB
  GO:0005524   F:ATP binding IDA:EcoCyc
  GO:0016887   F:ATPase activity IDA:EcoCyc
  GO:0042802   F:identical protein binding IPI:IntAct
  GO:0051082   F:unfolded protein binding IMP:EcoCyc
  GO:0006200   P:ATP catabolic process IDA:GOC
  GO:0007049   P:cell cycle IEA:UniProtKB-KW
  GO:0051301   P:cell division IEA:UniProtKB-KW
  GO:0006457   P:protein folding IMP:EcoCyc
  GO:0042026   P:protein refolding IEA:UniProtKB-HAMAP
  GO:0009408   P:response to heat IEP:EcoliWiki
  GO:0019068   P:virion assembly IMP:EcoliWiki
  IPR018370   Chaperonin_Cpn60_CS.
  IPR001844   Chaprnin_Cpn60.
  IPR002423   Cpn60/TCP-1.
  IPR027409   GroEL-like_apical_dom.
  IPR027413   GROEL-like_equatorial.
  PF00118   Cpn60_TCP1.
  PS00296   CHAPERONINS_CPN60.
  PR00298   CHAPERONIN60.