ID   DNLI_BPT6               Reviewed;         487 AA.
AC   P19088;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=30;
OS   Enterobacteria phage T6 (Bacteriophage T6).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus;
OC   Enterobacteria virus T6.
OX   NCBI_TaxID=10666;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3402337;
RA   Kaliman A.V., Zimin A.A., Nazipova N.N., Kryukov V.M., Tanyashin V.I.,
RA   Kraev A.S., Mironova M.V., Skyrabin K.G., Baev A.A.;
RT   "Comparative analysis of DNA-ligase genes of phages T6 and T4.";
RL   Dokl. Akad. Nauk SSSR 299:737-742(1988).
CC   -!- FUNCTION: DNA ligase, which is expressed in the early stage of lytic
CC       development, has been implicated in T4 DNA synthesis and genetic
CC       recombination. It may also play a role in T4 DNA repair.
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   -!- SUBUNIT: Interacts with the sliding clamp.
CC       {ECO:0000250|UniProtKB:P00970}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; M38465; AAA32562.1; -; Genomic_DNA.
DR   PIR; S06464; S06464.
DR   SMR; P19088; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication;
KW   Ligase; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..487
FT                   /note="DNA ligase"
FT                   /id="PRO_0000059596"
FT   REGION          229..237
FT                   /note="Interaction with the sliding clamp"
FT                   /evidence="ECO:0000250|UniProtKB:P00970"
FT   ACT_SITE        159
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT   BINDING         164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   487 AA;  55267 MW;  D560AF09145C6E3B CRC64;
     MILKILNEIA SIGSTKQKQA ILEKNKDNEL LKRVYRLTYS RGLQYYIKKW PKPGIATQSF
     GMLTLTDMLD FIEFTLATRK LTGNAAIEEL TGYITDGKKD DVEVLRRVMM RDLECGASVS
     IANKVWPGLI PEQPQMLASS YDEKGINKNI KFPAFAQLKA DGARCFAEVR GDELDDVRLL
     SRAGNEYLGL DLLKEELIKM TAEARQIHPE GVLIDGELVY HEQVKKEPEG LDFLFDAHPE
     NSKVKDFTEV AESRTASNGI ANKSLKGTIS EKEAQCMKFQ VWDYVPLVEV YGLPAFRLKY
     DVRFSKLEQM TSGYDKVILI ENQVVNNLDE AKVIYKKYID QGLEGIILKN IDGLWENARS
     KNLYKFKEVI DVDLKIVGIY PHRKDPTKAG GFILESECGK IKVNAGSGLK DKAGVKSHEL
     DRTRIMENQN YYIGKILECE CNGWLKSDGR TDYVKLFLPI AIRLREDKTK ANTFEDVFGD
     FHEVTGL