CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006320
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein 78, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 HSP78 
Gene Synonyms/Alias
 YDR258C; YD9320A.08C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
113TKLARDGKLDPVIGRacetylation[1]
349SKPDEIQKLDRAIMKacetylation[1]
366IELESLKKETDPVSVacetylation[1]
474VTSDDISKVVAKMTGacetylation[1]
576DMSEFQEKHTVSRLIacetylation[1]
792RVVVKDTKLVVLPNHacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Required, in concert with mitochondrial Hsp70 (SSC1), for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp70 chaperone system. Required for resumption of mitochondrial respiratory function, DNA synthesis and morphology after heat stress. Its main role may be maintaining the molecular chaperone SSC1 in a soluble and functional state. Also required for the efficient degradation of proteins by matrix protease PIM1, independent on its protein remodeling activity. 
Sequence Annotation
 NP_BIND 143 150 ATP 1 (Potential).
 NP_BIND 541 548 ATP 2 (Potential).
 REGION 98 344 NBD1.
 REGION 467 658 NBD2.  
Keyword
 ATP-binding; Chaperone; Coiled coil; Complete proteome; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Reference proteome; Repeat; Stress response; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 811 AA 
Protein Sequence
MLRQATKAPI QKYLQRTQLL RRSTPRIYTI VQCKRSICSF NARPRVANKL LSDIKTNALN 60
EVAISTCALK SSYGLPNFKR TYVQMRMDPN QQPEKPALEQ FGTNLTKLAR DGKLDPVIGR 120
DEEIARAIQI LSRRTKNNPC LIGRAGVGKT ALIDGLAQRI VAGEVPDSLK DKDLVALDLG 180
SLIAGAKYRG EFEERLKKVL EEIDKANGKV IVFIDEVHML LGLGKTDGSM DASNILKPKL 240
ARGLRCISAT TLDEFKIIEK DPALSRRFQP ILLNEPSVSD TISILRGLKE RYEVHHGVRI 300
TDTALVSAAV LSNRYITDRF LPDKAIDLVD EACAVLRLQH ESKPDEIQKL DRAIMKIQIE 360
LESLKKETDP VSVERREALE KDLEMKNDEL NRLTKIWDAE RAEIESIKNA KANLEQARIE 420
LEKCQREGDY TKASELRYSR IPDLEKKVAL SEKSKDGDKV NLLHDSVTSD DISKVVAKMT 480
GIPTETVMKG DKDRLLYMEN SLKERVVGQD EAIAAISDAV RLQRAGLTSE KRPIASFMFL 540
GPTGTGKTEL TKALAEFLFD DESNVIRFDM SEFQEKHTVS RLIGAPPGYV LSESGGQLTE 600
AVRRKPYAVV LFDEFEKAHP DVSKLLLQVL DEGKLTDSLG HHVDFRNTII VMTSNIGQDI 660
LLNDTKLGDD GKIDTATKNK VIEAMKRSYP PEFINRIDDI LVFNRLSKKV LRSIVDIRIA 720
EIQDRLAEKR MKIDLTDEAK DWLTDKGYDQ LYGARPLNRL IHRQILNSMA TFLLKGQIRN 780
GETVRVVVKD TKLVVLPNHE EGEVVEEEAE K 811 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IDA:SGD.
 GO:0051787; F:misfolded protein binding; IDA:SGD.
 GO:0034605; P:cellular response to heat; IMP:SGD.
 GO:0000002; P:mitochondrial genome maintenance; IGI:SGD.
 GO:0010892; P:positive regulation of mitochondrial translation in response to stress; IMP:SGD.
 GO:0030150; P:protein import into mitochondrial matrix; IGI:SGD.
 GO:0042026; P:protein refolding; IDA:SGD.
 GO:0050821; P:protein stabilization; IMP:SGD.
 GO:0043335; P:protein unfolding; IMP:SGD. 
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.