CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006767
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isoaspartyl peptidase 
Protein Synonyms/Alias
 Beta-aspartyl-peptidase; EcAIII; Isoaspartyl dipeptidase; Isoaspartyl peptidase subunit alpha; Isoaspartyl peptidase subunit beta 
Gene Name
 iaaA 
Gene Synonyms/Alias
 spt; ybiK; b0828; JW0812 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
174SGAPLDEKQKMGTVGacetylation[1]
314TTGIYREKGDTVATQacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L- isoaspartyl-containing di- and maybe also tripeptides. Also has L- asparaginase activity, although this may not be its principal function. 
Sequence Annotation
 REGION 207 210 Substrate binding.
 REGION 230 233 Substrate binding.
 ACT_SITE 179 179 Nucleophile.  
Keyword
 3D-structure; Autocatalytic cleavage; Complete proteome; Direct protein sequencing; Hydrolase; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 321 AA 
Protein Sequence
MGKAVIAIHG GAGAISRAQM SLQQELRYIE ALSAIVETGQ KMLEAGESAL DVVTEAVRLL 60
EECPLFNAGI GAVFTRDETH ELDACVMDGN TLKAGAVAGV SHLRNPVLAA RLVMEQSPHV 120
MMIGEGAENF AFARGMERVS PEIFSTSLRY EQLLAARKEG ATVLDHSGAP LDEKQKMGTV 180
GAVALDLDGN LAAATSTGGM TNKLPGRVGD SPLVGAGCYA NNASVAVSCT GTGEVFIRAL 240
AAYDIAALMD YGGLSLAEAC ERVVMEKLPA LGGSGGLIAI DHEGNVALPF NTEGMYRAWG 300
YAGDTPTTGI YREKGDTVAT Q 321 
Gene Ontology
 GO:0004067; F:asparaginase activity; IDA:EcoCyc.
 GO:0008798; F:beta-aspartyl-peptidase activity; IDA:EcoCyc.
 GO:0016540; P:protein autoprocessing; IMP:EcoCyc.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR000246; Peptidase_T2. 
Pfam
 PF01112; Asparaginase_2 
SMART
  
PROSITE
  
PRINTS