GenomeNet

Database: UniProt/SWISS-PROT
Entry: LIGC2_MYCS2
LinkDB: LIGC2_MYCS2
Original site: LIGC2_MYCS2 
ID   LIGC2_MYCS2             Reviewed;         354 AA.
AC   A0R5T3;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   10-APR-2019, entry version 81.
DE   RecName: Full=DNA ligase C2;
DE            EC=6.5.1.1;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=ligC2; OrderedLocusNames=MSMEG_6304, MSMEI_6138;
OS   Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through
RT   orthology and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=15778718; DOI=10.1038/nsmb915;
RA   Gong C., Bongiorno P., Martins A., Stephanou N.C., Zhu H., Shuman S.,
RA   Glickman M.S.;
RT   "Mechanism of nonhomologous end-joining in mycobacteria: a low-
RT   fidelity repair system driven by Ku, ligase D and ligase C.";
RL   Nat. Struct. Mol. Biol. 12:304-312(2005).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18281464; DOI=10.1101/gad.1631908;
RA   Aniukwu J., Glickman M.S., Shuman S.;
RT   "The pathways and outcomes of mycobacterial NHEJ depend on the
RT   structure of the broken DNA ends.";
RL   Genes Dev. 22:512-527(2008).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair (By
CC       similarity). Has weak intrinsic nick joining activities and
CC       accumulates DNA-adenylate. Acts as a backup for LigD in the Ku-
CC       LigD-dependent NHEJ pathway. {ECO:0000250,
CC       ECO:0000269|PubMed:18281464}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1;
CC   -!- DISRUPTION PHENOTYPE: Not essential; a double ligC1-ligC2 mutant
CC       grows normally, no effect on NHEJ. In a triple deletion with ligD
CC       NHEJ on blunt-ended plasmid is 90-fold impaired. In quadruple
CC       ligB-ligC1-ligC2-ligD deletions NHEJ on blunt and 5'-overhangs is
CC       0.22 and 0.12% of wild-type respectively; only 4-fold decrease in
CC       3'-overhang NHEJ. {ECO:0000269|PubMed:15778718,
CC       ECO:0000269|PubMed:18281464}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; CP000480; ABK75022.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42568.1; -; Genomic_DNA.
DR   RefSeq; WP_011731191.1; NZ_CP009494.1.
DR   RefSeq; YP_890521.1; NC_008596.1.
DR   ProteinModelPortal; A0R5T3; -.
DR   SMR; A0R5T3; -.
DR   STRING; 246196.MSMEI_6138; -.
DR   EnsemblBacteria; ABK75022; ABK75022; MSMEG_6304.
DR   EnsemblBacteria; AFP42568; AFP42568; MSMEI_6138.
DR   GeneID; 4537064; -.
DR   KEGG; msb:LJ00_31160; -.
DR   KEGG; msg:MSMEI_6138; -.
DR   KEGG; msm:MSMEG_6304; -.
DR   PATRIC; fig|246196.19.peg.6139; -.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000222508; -.
DR   OMA; AGFRWHK; -.
DR   OrthoDB; 1073940at2; -.
DR   BioCyc; GCF_000015005:MSMEG_6304-MONOMER; -.
DR   BioCyc; MSME246196:G1H7P-6270-MONOMER; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    354       DNA ligase C2.
FT                                /FTId=PRO_0000425952.
FT   ACT_SITE     29     29       N6-AMP-lysine intermediate.
FT                                {ECO:0000250}.
SQ   SEQUENCE   354 AA;  39324 MW;  63D2ADAF94BE7F63 CRC64;
     MDLPVLPPVS PMLSKSVNQI PPGMSYEPKW DGFRSILFRD GAEVELGSRK ERPMTRYFPE
     LVAAALTELP DRCVIDGEIV LPADNHLDFE ALQLRLHPAA SRVAMLAEQT PAAFIAFDLL
     ALGDDDYTGR PFSERRAALE TALADAGPTF HLTPATTDLP TAQRWFHEFE GAGLDGVIAK
     PLDLTYQPDK RVMFKVKHQR TADCVVAGYR LHKSGADAVG SLLLGLYDDD GSLASVGVIG
     AFPMATRRAL FTELQTLVAD FDHHPWNWAA QAAADPELAR RYGGGSRWNA GKDLSFVPLR
     PERLVEVRYD HMEGRRFRHT AQFNRWRPDR DARSCTFAQL DSPPHSSSVT SCRV
//
DBGET integrated database retrieval system