| Tag | Content |
|---|
| CPLM ID | CPLM-022785 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Chaperone protein ClpB |
Protein Synonyms/Alias | |
Gene Name | clpB |
Gene Synonyms/Alias | TTHA1487 |
Created Date | July 27, 2013 |
Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
NCBI Taxa ID | 300852 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 347 | ILRGLKEKYEVHHGV | acetylation | [1] | | 448 | KLTEEIAKLRAEWER | acetylation | [1] | | 510 | EVEALSEKLRGARFV | acetylation | [1] | | 558 | RLEEELHKRVVGQDE | acetylation | [1] | | 630 | DMTEYMEKHAVSRLI | acetylation | [1] |
|
Reference | [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. Okanishi H, Kim K, Masui R, Kuramitsu S. J Proteome Res. 2013 Aug 1;. [ PMID: 23901841] |
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. |
Sequence Annotation | NP_BIND 198 205 ATP 1.
NP_BIND 595 602 ATP 2.
REGION 1 135 N-terminal.
REGION 151 331 NBD1.
REGION 332 535 Linker.
REGION 545 756 NBD2.
REGION 757 854 C-terminal. |
Keyword | 3D-structure; ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome; Repeat; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 854 AA |
Protein Sequence | MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DERSLAWRLL EKAGADPKAL 60
KELQERELAR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE LKDRYVAVDT LVLALAEATP 120
GLPGLEALKG ALKELRGGRT VQTEHAESTY NALEQYGIDL TRLAAEGKLD PVIGRDEEIR 180
RVIQILLRRT KNNPVLIGEP GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG 240
AKYRGEFEER LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL 300
RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV HHGVRISDSA 360
IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP EEIDALERKK LQLEIEREAL 420
KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR AEWEREREIL RKLREAQHRL DEVRREIELA 480
ERQYDLNRAA ELRYGELPKL EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK 540
LLEGEREKLL RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG 600
KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG QLTEAVRRRP 660
YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR NTVIILTSNL GSPLILEGLQ 720
KGWPYERIRD EVFKVLQQHF RPEFLNRLDE IVVFRPLTKE QIRQIVEIQL SYLRARLAEK 780
RISLELTEAA KDFLAERGYD PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG 840
PAGLVFAVPA RVEA 854 |
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:0016485; P:protein processing; IEA:InterPro. GO:0009408; P:response to heat; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |