※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chaperone protein ClpB
Protein Synonyms/Alias
 
Gene Name
 clpB
Gene Synonyms/Alias
 htpM; OrderedLocusNames=Z3886, ECs3455
Created Date
 3-June-2014
Organism
 Escherichia coli O157:H7
NCBI Taxa ID
 83334
Phosphorylation
Position
Peptide
Code
Type
References
503 ARMSELQYGKIPELE Y HTP [1]
661 VGYEEGGYLTEAVRR Y HTP [1]
656 APPGYVGYEEGGYLT Y HTP [1]
653 LVGAPPGYVGYEEGG Y HTP [1]
Reference
 [1]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: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity)
Sequence Annotation From UniProt
 COILED 391 525 By similarity
 MOD_RES 96 96 N6-acetyllysine (By similarity)
 MOD_RES 176 176 N6-acetyllysine (By similarity)
 MOD_RES 640 640 N6-acetyllysine (By similarity)
Key Word From UniProt
 Acetylation; ATP-binding; Chaperone; Coiledcoil; Completeproteome; Cytoplasm; Nucleotide-binding; Repeat; Stressresponse
Protein Sequence
 MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL TSAGINAGQL 60
 RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK RGDNFISSEL FVLAALESRG 120
 TLADILKAAG ATTANITQAI EQMRGGESVN DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV 180
 IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL 240
 DMGALVAGAK YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK 300
 PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL RGLKERYELH 360
 HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE ELDRLDRRII 420
 QLKLEQQALM KESDEASKKR LDMLNEELSD KERQYSELEE EWKAEKASLS GTQTIKAELE 480
 QAKIAIEQAR RVGDLARMSE LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL 540
 ARWTGIPVSR MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS 600
 FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG 660
 YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL 720
 GSDLIQERFG ELDYAHMKEL VLGVVSHNFR PEFINRIDEV VVFHPLGEQH IASIAQIQLK 780
 RLYKRLEERG YEIHISDEAL KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP 840
 GKVIRLEVNE DRIVAVQ 857
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  GO:0005524   F:ATP binding IEA:UniProtKB-KW
  GO:0017111   F:nucleoside-triphosphatase activity IEA:InterPro
  GO:0016485   P:protein processing IEA:InterPro
  GO:0009408   P:response to heat IEA:InterPro
  IPR003593   AAA+_ATPase.
  IPR003959   ATPase_AAA_core.
  IPR017730   Chaperonin_ClpB.
  IPR019489   Clp_ATPase_C.
  IPR004176   Clp_N.
  IPR001270   ClpA/B.
  IPR018368   ClpA/B_CS1.
  IPR028299   ClpA/B_CS2.
  IPR023150   Dbl_Clp-N.
  IPR027417   P-loop_NTPase.
  PF00004   AAA.
  PF07724   AAA_2.
  PF02861   Clp_N.
  PF10431   ClpB_D2-small.
  SM00382   AAA.
  SM01086   ClpB_D2-small.
  PS00870   CLPAB_1.
  PS00871   CLPAB_2.
  PR00300   CLPPROTEASEA.