※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperone protein HtpG
Protein Synonyms/Alias
 
Gene Name
 htpG
Gene Synonyms/Alias
 b0473, JW0462
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
410 ASTHTDSSAQTVSLE S HTP [1]
405 KLLRFASTHTDSSAQ T HTP [1]
409 FASTHTDSSAQTVSL S HTP [1]
404 AKLLRFASTHTDSSA S HTP [1]
407 LRFASTHTDSSAQTV T HTP [1]
104 IAKSGTKSFLESLGS S HTP [1]
500 LADEVDESAKEAEKA S HTP [2]
239 ALWTRNKSEITDEEY S HTP [2]
108 GTKSFLESLGSDQAK S HTP [2]
220 REEKDGETVISWEKI T HTP [2]
57 ALSNPDLYEGDGELR Y HTP [3]
Reference
 [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation.
 Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M
 Mol. Cell Proteomics 2008, Feb;7(2):299-307. [PMID:17938405]
 [2]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]
 [3]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: Molecular chaperone. Has ATPase activity
Sequence Annotation From UniProt
 
Key Word From UniProt
 3D-structure; ATP-binding; Cellinnermembrane; Cellmembrane; Chaperone; Completeproteome; Cytoplasm; Directproteinsequencing; Membrane; Nucleotide-binding; Phosphoprotein; Referenceproteome; Stressresponse
Protein Sequence
 MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD 60
 GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS GTKSFLESLG SDQAKDSQLI 120
 GQFGVGFYSA FIVADKVTVR TRAAGEKPEN GVFWESAGEG EYTVADITKE DRGTEITLHL 180
 REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE 240
 ITDEEYKEFY KHIAHDFNDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY 300
 VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN ALTKRVLQML 360
 EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL RFASTHTDSS AQTVSLEDYV 420
 SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF 480
 QSVSKVDESL EKLADEVDES AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS 540
 TDADEMSTQM AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA 600
 LLAERGTLED PNLFIRRMNQ LLVS 624
  GO:0005829   C:cytosol IDA:UniProtKB
  GO:0005886   C:plasma membrane IEA:UniProtKB-SubCell
  GO:0005524   F:ATP binding IEA:UniProtKB-HAMAP
  GO:0042623   F:ATPase activity, coupled IDA:EcoCyc
  GO:0042802   F:identical protein binding IPI:IntAct
  GO:0006200   P:ATP catabolic process IDA:GOC
  GO:0006974   P:cellular response to DNA damage stimulus IEP:EcoliWiki
  GO:0006457   P:protein folding EXP:EcoCyc
  GO:0009408   P:response to heat IEP:EcoliWiki
  IPR003594   HATPase_ATP-bd.
  IPR019805   Heat_shock_protein_90_CS.
  IPR001404   Hsp90_fam.
  IPR020575   Hsp90_N.
  IPR020568   Ribosomal_S5_D2-typ_fold.
  PF02518   HATPase_c.
  PF00183   HSP90.
  SM00387   HATPase_c.
  PS00298   HSP90.
  PR00775   HEATSHOCK90.