CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010066
UniProt Accession
Genbank Protein ID
 U00089 
Genbank Nucleotide ID
Protein Name
 Chaperone protein ClpB 
Protein Synonyms/Alias
  
Gene Name
 clpB 
Gene Synonyms/Alias
 MPN_531; MP311 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
28SINDEVLKNKVDPIIacetylation[1]
191ALERRFQKILVSEPSacetylation[1]
286ETEYAALKQDKENADacetylation[1]
323DSLTAEWKKEKTNFEacetylation[1]
368ILYYDIPKLKNQLEQacetylation[1]
417KKLLETEKEKLLHLGacetylation[1]
561VLDDGTLKDSQGRLVacetylation[1]
684QIATLIAKQILEGIIacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819
Functional Description
 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
 NP_BIND 60 67 ATP 1 (By similarity).
 NP_BIND 466 473 ATP 2 (By similarity).
 REGION 14 196 NBD1 (By similarity).
 REGION 197 406 Linker (By similarity).
 REGION 416 618 NBD2 (By similarity).
 REGION 619 715 C-terminal (By similarity).  
Keyword
 ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome; Repeat; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 715 AA 
Protein Sequence
MDFSFTPTPD KRDFLKEMGR SINDEVLKNK VDPIIGRDNE IRRLIEILSR KNKNNPVLIG 60
EPGVGKTAIV EGFVRRVVNN DVPLNLRDVE IYELSLSGLI AGTQYQGEFE KRVNGILKQV 120
KESNGKIILF IDEIHQIVGL GRNSSSGAMD IANILKPMLA RGEIKVIGAT TLKEYREYVE 180
KDGALERRFQ KILVSEPSQQ EALTIMRGLK TRWELFHNLT IFDSALVAAV EMSARYIPDR 240
NLPDKAIDLI DEASAKIKTE MASEPVVIDT LKREIINLET EYAALKQDKE NADNKKKQGH 300
LDNLKQQLDE LKKKRDSLTA EWKKEKTNFE SINKLKKEIE DLQTRLELYQ TEGNYEAASK 360
ILYYDIPKLK NQLEQAQKKY VDSKHDLFKT EVSENEVAEV VSQATGIPLK KLLETEKEKL 420
LHLGDEIKKR VKGQDAAVET VVNTVMRGRV NLNDPNRPIG SFIFLGSTGV GKTELAKSLA 480
EVLFDNEKAM IRFDMSEYME KHSVAKLIGA PPGYVGYEQS GLLTEAVRRK PYCVLLFDEI 540
EKAHPDVTNI LLQVLDDGTL KDSQGRLVNF KNTMIIMTSN LGSNYIMENK RDLAMEALKK 600
HFRAEFINRI DEIVFFSVLQ KTTVLEIITN LLDQLNQRLA KQNLKFTFDP KLNEFIYKSS 660
FDEQFGARPI KRFIDRQIAT LIAKQILEGI ITKDVSYNVI VEKDKVAIVA NKVKS 715 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR013093; ATPase_AAA-2.
 IPR003959; ATPase_AAA_core.
 IPR018368; Chaperonin_ClpA/B_CS.
 IPR001270; Chaprnin_ClpA/B.
 IPR019489; Clp_ATPase_C.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA
 PF07724; AAA_2
 PF10431; ClpB_D2-small 
SMART
 SM00382; AAA
 SM01086; ClpB_D2-small 
PROSITE
 PS00870; CLPAB_1
 PS00871; CLPAB_2 
PRINTS
 PR00300; CLPPROTEASEA.