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Database: UniProt/SWISS-PROT
Entry: LIGC1_MYCS2
LinkDB: LIGC1_MYCS2
Original site: LIGC1_MYCS2 
ID   LIGC1_MYCS2             Reviewed;         348 AA.
AC   A0R5T2;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   13-FEB-2019, entry version 82.
DE   RecName: Full=DNA ligase C1;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=ligC; OrderedLocusNames=MSMEG_6302, MSMEI_6137;
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   FUNCTION, COFACTOR, AND SUBUNIT.
RX   PubMed=14985346; DOI=10.1074/jbc.M401841200;
RA   Gong C., Martins A., Bongiorno P., Glickman M., Shuman S.;
RT   "Biochemical and genetic analysis of the four DNA ligases of
RT   mycobacteria.";
RL   J. Biol. Chem. 279:20594-20606(2004).
RN   [5]
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   [6]
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:14985346, 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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10135};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
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; ABK76125.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42567.1; -; Genomic_DNA.
DR   RefSeq; WP_011731190.1; NZ_CP009494.1.
DR   RefSeq; YP_890520.1; NC_008596.1.
DR   ProteinModelPortal; A0R5T2; -.
DR   SMR; A0R5T2; -.
DR   STRING; 246196.MSMEG_6302; -.
DR   EnsemblBacteria; ABK76125; ABK76125; MSMEG_6302.
DR   EnsemblBacteria; AFP42567; AFP42567; MSMEI_6137.
DR   GeneID; 4533888; -.
DR   KEGG; msg:MSMEI_6137; -.
DR   KEGG; msm:MSMEG_6302; -.
DR   PATRIC; fig|246196.19.peg.6138; -.
DR   eggNOG; ENOG4105GN4; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000222508; -.
DR   OMA; YRPHKSQ; -.
DR   BioCyc; GCF_000015005:MSMEG_6302-MONOMER; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
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; PS00697; DNA_LIGASE_A1; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Ligase; Reference proteome.
FT   CHAIN         1    348       DNA ligase C1.
FT                                /FTId=PRO_0000425951.
FT   ACT_SITE     32     32       N6-AMP-lysine intermediate.
FT                                {ECO:0000305}.
SQ   SEQUENCE   348 AA;  39495 MW;  84664C237963598C CRC64;
     MDLPVQPPIE PMLAKAQVKV PDEAGVWSYE PKWDGFRALV FRDGDDVVLQ SRNGKDLGRY
     FPELLDALRD ELVEKCVLDG EVVVPRDIAG RVRLDWESLS QRIHPAASRI KMLAEQTPAH
     FIGFDALALG DRSLLKEPFR VRREALAEAV DNKRWCHVTR TSEDPALGTE WLKTFEGAGL
     DGVIAKRLDG PYLPGKREMV KVKHHRDADC VAMGYRIHKS GDGIGSILLG LYRDDGELQM
     VGGAASFTAK DRIKLLAELE PLREGDEMRE GDPSRWNSAA DKRWTPLRPE KVCEVAYDQM
     EGNSVEGRRF RHAVKFLRWR PDREPSSCTF DQLDTPLNYD LYDVLEEQ
//
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