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Database: UniProt/SWISS-PROT
Entry: DNLI_MYCTO
LinkDB: DNLI_MYCTO
Original site: DNLI_MYCTO 
ID   DNLI_MYCTO              Reviewed;         507 AA.
AC   P9WNV4; L0TBG5; P95096; Q7D671;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 24.
DE   RecName: Full=DNA ligase B;
DE            Short=LigB;
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=ligB; OrderedLocusNames=MT3148;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
DR   EMBL; AE000516; AAK47481.1; -; Genomic_DNA.
DR   PIR; G70649; G70649.
DR   RefSeq; WP_003415991.1; NZ_KK341227.1.
DR   ProteinModelPortal; P9WNV4; -.
DR   SMR; P9WNV4; -.
DR   EnsemblBacteria; AAK47481; AAK47481; MT3148.
DR   KEGG; mtc:MT3148; -.
DR   PATRIC; fig|83331.31.peg.3392; -.
DR   KO; K10747; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
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; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN         1    507       DNA ligase B.
FT                                /FTId=PRO_0000427061.
FT   REGION        1    172       Not required for adenylyltransferase
FT                                activity, required for nick joining.
FT   ACT_SITE    211    211       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     209    209       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     216    216       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     231    231       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     260    260       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     372    372       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     378    378       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   507 AA;  53727 MW;  8D73EB4C08C7149D CRC64;
     MLLHDVAITS MDVAATSSRL TKVARIAALL HRAAPDTQLV TIIVSWLSGE LPQRHIGVGW
     AALRSLPPPA PQPALTVTGV DATLSKIGTL SGKGSQAQRA ALVAELFSAA TEAEQTFLLR
     LLGGELRQGA KGGIMADAVA QAAGLPAATV QRAAMLGGDL AAAAAAGLSG AALDTFTLRV
     GRPIGPMLAQ TATSVHDALE RHGGTTIFEA KLDGARVQIH RANDQVRIYT RSLDDVTARL
     PEVVEATLAL PVRDLVADGE AIALCPDNRP QRFQVTASRF GRSVDVAAAR ATQPLSVFFF
     DILHRDGTDL LEAPTTERLA ALDALVPARH RVDRLITSDP TDAANFLDAT LAAGHEGVMA
     KAPAARYLAG RRGAGWLKVK PVHTLDLVVL AVEWGSGRRR GKLSNIHLGA RDPATGGFVM
     VGKTFKGMTD AMLDWQTTRF HEIAVGPTDG YVVQLRPEQV VEVALDGVQR SSRYPGGLAL
     RFARVVRYRA DKDPAEADTI DAVRALY
//
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