CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002728
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exodeoxyribonuclease III 
Protein Synonyms/Alias
 EXO III; Exonuclease III; AP endonuclease VI 
Gene Name
 xthA 
Gene Synonyms/Alias
 xth; b1749; JW1738 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
24QLEAIVEKHQPDVIGacetylation[1]
36VIGLQETKVHDDMFPacetylation[1]
49FPLEEVAKLGYNVFYacetylation[1]
70YGVALLTKETPIAVRacetylation[1]
121ESRDHPIKFPAKAQFacetylation[1]
141NYLETELKRDNPVLIacetylation[1]
141NYLETELKRDNPVLIpupylation[2]
176KRWLRTGKCSFLPEEacetylation[1]
255YEIRSMEKPSDHAPVacetylation[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]
 [2] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222
Functional Description
 Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities. 
Sequence Annotation
 ACT_SITE 109 109 By similarity.
 ACT_SITE 151 151 Proton donor/acceptor (By similarity).
 METAL 34 34 Magnesium 1 (By similarity).
 METAL 151 151 Magnesium 2 (By similarity).
 METAL 153 153 Magnesium 2 (By similarity).
 METAL 258 258 Magnesium 1 (By similarity).  
Keyword
 3D-structure; Complete proteome; DNA damage; DNA repair; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 268 AA 
Protein Sequence
MKFVSFNING LRARPHQLEA IVEKHQPDVI GLQETKVHDD MFPLEEVAKL GYNVFYHGQK 60
GHYGVALLTK ETPIAVRRGF PGDDEEAQRR IIMAEIPSLL GNVTVINGYF PQGESRDHPI 120
KFPAKAQFYQ NLQNYLETEL KRDNPVLIMG DMNISPTDLD IGIGEENRKR WLRTGKCSFL 180
PEEREWMDRL MSWGLVDTFR HANPQTADRF SWFDYRSKGF DDNRGLRIDL LLASQPLAEC 240
CVETGIDYEI RSMEKPSDHA PVWATFRR 268 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0004519; F:endonuclease activity; IEA:InterPro.
 GO:0008853; F:exodeoxyribonuclease III activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006974; P:response to DNA damage stimulus; IDA:EcoCyc. 
Interpro
 IPR020847; AP_endonuclease_F1_BS.
 IPR020848; AP_endonuclease_F1_CS.
 IPR005135; Endo/exonuclease/phosphatase.
 IPR004808; ExoDNase_III. 
Pfam
 PF03372; Exo_endo_phos 
SMART
  
PROSITE
 PS00726; AP_NUCLEASE_F1_1
 PS00727; AP_NUCLEASE_F1_2
 PS00728; AP_NUCLEASE_F1_3
 PS51435; AP_NUCLEASE_F1_4 
PRINTS