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Database: UniProt/SWISS-PROT
Entry: LIGC_MYCTU
LinkDB: LIGC_MYCTU
Original site: LIGC_MYCTU 
ID   LIGC_MYCTU              Reviewed;         358 AA.
AC   L0TDE1;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=DNA ligase C;
DE            EC=6.5.1.1;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=ligC; OrderedLocusNames=Rv3731;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC       replication, DNA recombination and DNA repair. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- DISRUPTION PHENOTYPE: Not essential for growth (in strain Erdman).
CC       {ECO:0000269|PubMed:14985346}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP46558.1; -; Genomic_DNA.
DR   RefSeq; NP_218248.1; NC_000962.3.
DR   RefSeq; WP_003917239.1; NZ_NVQJ01000009.1.
DR   AlphaFoldDB; L0TDE1; -.
DR   SMR; L0TDE1; -.
DR   STRING; 83332.Rv3731; -.
DR   PaxDb; 83332-Rv3731; -.
DR   DNASU; 885771; -.
DR   GeneID; 885771; -.
DR   KEGG; mtu:Rv3731; -.
DR   TubercuList; Rv3731; -.
DR   eggNOG; COG1793; Bacteria.
DR   InParanoid; L0TDE1; -.
DR   OrthoDB; 9770771at2; -.
DR   PhylomeDB; L0TDE1; -.
DR   Proteomes; UP000001584; 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   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..358
FT                   /note="DNA ligase C"
FT                   /id="PRO_0000425953"
FT   ACT_SITE        29
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  40160 MW;  8EBA33D1A57CAA4E CRC64;
     MQLPVMPPVS PMLAKSVTAI PPDASYEPKW DGFRSICFRD GDQVELGSRN ERPMTRYFPE
     LVAAIRAELP HRCVIDGEII IATDHGLDFE ALQQRIHPAE SRVRMLADRT PASFIAFDLL
     ALGDDDYTGR PFSERRAALV DAVTGSGADA DLSIHVTPAT TDMATAQRWF SEFEGAGLDG
     VIAKPPHITY QPDKRVMFKI KHLRTADCVV AGYRVHKSGS DAIGSLLLGL YQEDGQLASV
     GVIGAFPMAE RRRLLTELQP LVTSFDDHPW NWAAHVAGQR TPRKNEFSRW NVGKDLSFVP
     LRPERVVEVR YDRMEGARFR HTAQFNRWRP DRDPRSCSYA QLERPLTVSL SDIVPGLR
//
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