Tag | Content |
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CPLM ID | CPLM-010066 |
UniProt Accession | |
Genbank Protein ID | |
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 |
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28 | SINDEVLKNKVDPII | acetylation | [1] | 191 | ALERRFQKILVSEPS | acetylation | [1] | 286 | ETEYAALKQDKENAD | acetylation | [1] | 323 | DSLTAEWKKEKTNFE | acetylation | [1] | 368 | ILYYDIPKLKNQLEQ | acetylation | [1] | 417 | KKLLETEKEKLLHLG | acetylation | [1] | 561 | VLDDGTLKDSQGRLV | acetylation | [1] | 684 | QIATLIAKQILEGII | acetylation | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |