DNLI_BPT4
ID DNLI_BPT4 Reviewed; 487 AA.
AC P00970;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6314278; DOI=10.1093/nar/11.20.7145;
RA Armstrong J., Brown R.S., Tsugita A.;
RT "Primary structure and genetic organization of phage T4 DNA ligase.";
RL Nucleic Acids Res. 11:7145-7156(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3] {ECO:0007744|PDB:5WFY, ECO:0007744|PDB:6DRT, ECO:0007744|PDB:6DT1}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-129 IN COMPLEX WITH DNA, AND
RP INTERACTION WITH THE VIRAL SLIDING CLAMP.
RX PubMed=30169742; DOI=10.1093/nar/gky776;
RA Shi K., Bohl T.E., Park J., Zasada A., Malik S., Banerjee S., Tran V.,
RA Li N., Yin Z., Kurniawan F., Orellana K., Aihara H.;
RT "T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a
RT unique mode of sliding clamp interaction.";
RL Nucleic Acids Res. 46:10474-10488(2018).
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:0000269|PubMed:30169742}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; X00039; CAA24921.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42440.1; -; Genomic_DNA.
DR PIR; A01201; LQBP34.
DR RefSeq; NP_049813.1; NC_000866.4.
DR PDB; 5WFY; X-ray; 1.40 A; A=1-129.
DR PDB; 6DRT; X-ray; 2.12 A; D/E/F=225-237.
DR PDB; 6DT1; X-ray; 2.75 A; A/E=1-487.
DR PDBsum; 5WFY; -.
DR PDBsum; 6DRT; -.
DR PDBsum; 6DT1; -.
DR SMR; P00970; -.
DR BindingDB; P00970; -.
DR ChEMBL; CHEMBL5733; -.
DR GeneID; 1258680; -.
DR KEGG; vg:1258680; -.
DR PRO; PR:P00970; -.
DR Proteomes; UP000009087; Genome.
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:0003909; F:DNA ligase activity; IDA:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair;
KW DNA replication; Ligase; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..487
FT /note="DNA ligase"
FT /id="PRO_0000059595"
FT REGION 229..237
FT /note="Interaction with the sliding clamp"
FT /evidence="ECO:0000269|PubMed:30169742"
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"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:5WFY"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:5WFY"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5WFY"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:5WFY"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:5WFY"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:5WFY"
FT TURN 75..79
FT /evidence="ECO:0007829|PDB:5WFY"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:5WFY"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:5WFY"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5WFY"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:5WFY"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6DRT"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:6DT1"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 357..367
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 370..381
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 436..445
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:6DT1"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:6DT1"
FT HELIX 481..485
FT /evidence="ECO:0007829|PDB:6DT1"
SQ SEQUENCE 487 AA; 55293 MW; 39F8718DD067F8AA CRC64;
MILKILNEIA SIGSTKQKQA ILEKNKDNEL LKRVYRLTYS RGLQYYIKKW PKPGIATQSF
GMLTLTDMLD FIEFTLATRK LTGNAAIEEL TGYITDGKKD DVEVLRRVMM RDLECGASVS
IANKVWPGLI PEQPQMLASS YDEKGINKNI KFPAFAQLKA DGARCFAEVR GDELDDVRLL
SRAGNEYLGL DLLKEELIKM TAEARQIHPE GVLIDGELVY HEQVKKEPEG LDFLFDAYPE
NSKAKEFAEV AESRTASNGI ANKSLKGTIS EKEAQCMKFQ VWDYVPLVEI YSLPAFRLKY
DVRFSKLEQM TSGYDKVILI ENQVVNNLDE AKVIYKKYID QGLEGIILKN IDGLWENARS
KNLYKFKEVI DVDLKIVGIY PHRKDPTKAG GFILESECGK IKVNAGSGLK DKAGVKSHEL
DRTRIMENQN YYIGKILECE CNGWLKSDGR TDYVKLFLPI AIRLREDKTK ANTFEDVFGD
FHEVTGL
