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 27-MAR-2024, entry version 98.
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 Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 orthology
RT 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-fidelity
RT 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 structure of
RT the broken DNA ends.";
RL Genes Dev. 22:512-527(2008).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair (By similarity). Has weak
CC intrinsic nick joining activities and accumulates DNA-adenylate. Acts
CC as a backup for LigD in the Ku-LigD-dependent NHEJ pathway.
CC {ECO:0000250, 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 grows
CC normally, no effect on NHEJ. In a triple deletion with ligD NHEJ on
CC blunt-ended plasmid is 90-fold impaired. In quadruple ligB-ligC1-ligC2-
CC ligD deletions NHEJ on blunt and 5'-overhangs is 0.22 and 0.12% of
CC wild-type respectively; only 4-fold decrease in 3'-overhang NHEJ.
CC {ECO:0000269|PubMed:15778718, ECO:0000269|PubMed:18281464}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK75022.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42568.1; -; Genomic_DNA.
DR RefSeq; YP_890521.1; NC_008596.1.
DR AlphaFoldDB; A0R5T3; -.
DR SMR; A0R5T3; -.
DR STRING; 246196.MSMEG_6304; -.
DR PaxDb; 246196-MSMEI_6138; -.
DR KEGG; msg:MSMEI_6138; -.
DR KEGG; msm:MSMEG_6304; -.
DR PATRIC; fig|246196.19.peg.6139; -.
DR eggNOG; COG1793; Bacteria.
DR OrthoDB; 9770771at2; -.
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 CDD; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR CDD; cd07970; OBF_DNA_ligase_LigC; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR044119; Adenylation_LigC-like.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR044117; OBF_LigC-like.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..354
FT /note="DNA ligase C2"
FT /id="PRO_0000425952"
FT ACT_SITE 29
FT /note="N6-AMP-lysine intermediate"
FT /evidence="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
//
