DNLI_BPT7
ID DNLI_BPT7 Reviewed; 359 AA.
AC P00969;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135, ECO:0000269|PubMed:8653795};
DE AltName: Full=DNA ligase gp1.3;
DE AltName: Full=Gene product 1.3;
DE Short=Gp1.3;
GN OrderedLocusNames=1.3;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA Dunn J.J., Studier F.W.;
RT "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT the beginning of gene 4.";
RL J. Mol. Biol. 148:303-330(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-359.
RX PubMed=7001354; DOI=10.1093/nar/8.10.2119;
RA Dunn J.J., Studier F.W.;
RT "The transcription termination site at the end of the early region of
RT bacteriophage T7 DNA.";
RL Nucleic Acids Res. 8:2119-2132(1980).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=6254001; DOI=10.1073/pnas.77.7.3917;
RA Saito H., Tabor S., Tamanoi F., Richardson C.C.;
RT "Nucleotide sequence of the primary origin of bacteriophage T7 DNA
RT replication: relationship to adjacent genes and regulatory elements.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:3917-3921(1980).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF LYS-238 AND LYS-240.
RX PubMed=10656817; DOI=10.1006/jmbi.1999.3423;
RA Doherty A.J., Dafforn T.R.;
RT "Nick recognition by DNA ligases.";
RL J. Mol. Biol. 296:43-56(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ATP, CATALYTIC
RP ACTIVITY, AND DNA-BINDING.
RX PubMed=8653795; DOI=10.1016/s0092-8674(00)81260-x;
RA Subramanya H.S., Doherty A.J., Ashford S.R., Wigley D.B.;
RT "Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7.";
RL Cell 85:607-615(1996).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair in an ATP-dependent
CC reaction. Binds specifically to DNA nicks containing a 3'-OH and a 5'-
CC phosphate group. {ECO:0000269|PubMed:10656817}.
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, ECO:0000269|PubMed:8653795};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; V01124; CAA24322.1; -; Genomic_DNA.
DR EMBL; V01126; CAA24326.1; -; Genomic_DNA.
DR EMBL; V01127; CAA24336.1; -; Genomic_DNA.
DR EMBL; V01146; CAA24393.1; -; Genomic_DNA.
DR PIR; E94615; LQBP37.
DR RefSeq; NP_041963.1; NC_001604.1.
DR PDB; 1A0I; X-ray; 2.60 A; A=3-349.
DR PDBsum; 1A0I; -.
DR SMR; P00969; -.
DR MINT; P00969; -.
DR PRIDE; P00969; -.
DR GeneID; 1261055; -.
DR KEGG; vg:1261055; -.
DR BRENDA; 6.5.1.1; 736.
DR EvolutionaryTrace; P00969; -.
DR Proteomes; UP000000840; 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:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006266; P:DNA ligation; IEA:InterPro.
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 Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR041559; DNA_ligase_ATP-dep_T7_C.
DR InterPro; IPR016306; DNA_ligase_T7.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF17879; DNA_ligase_C; 1.
DR PIRSF; PIRSF001600; DNA_ligase_phage_T3; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair;
KW DNA replication; DNA-binding; Ligase; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..359
FT /note="DNA ligase"
FT /id="PRO_0000059598"
FT ACT_SITE 34
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 32..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:8653795"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:8653795"
FT BINDING 55..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:8653795"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:8653795"
FT BINDING 217
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:8653795"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:8653795"
FT MUTAGEN 238
FT /note="K->A: Complete loss of transadenylation activity."
FT /evidence="ECO:0000269|PubMed:10656817"
FT MUTAGEN 240
FT /note="K->A: About 99% loss of transadenylation activity."
FT /evidence="ECO:0000269|PubMed:10656817"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 87..99
FT /evidence="ECO:0007829|PDB:1A0I"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1A0I"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 167..184
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:1A0I"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:1A0I"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1A0I"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:1A0I"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1A0I"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1A0I"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:1A0I"
SQ SEQUENCE 359 AA; 41133 MW; 43DA453B71BDF8DC CRC64;
MMNIKTNPFK AVSFVESAIK KALDNAGYLI AEIKYDGVRG NICVDNTANS YWLSRVSKTI
PALEHLNGFD VRWKRLLNDD RCFYKDGFML DGELMVKGVD FNTGSGLLRT KWTDTKNQEF
HEELFVEPIR KKDKVPFKLH TGHLHIKLYA ILPLHIVESG EDCDVMTLLM QEHVKNMLPL
LQEYFPEIEW QAAESYEVYD MVELQQLYEQ KRAEGHEGLI VKDPMCIYKR GKKSGWWKMK
PENEADGIIQ GLVWGTKGLA NEGKVIGFEV LLESGRLVNA TNISRALMDE FTETVKEATL
SQWGFFSPYG IGDNDACTIN PYDGWACQIS YMEETPDGSL RHPSFVMFRG TEDNPQEKM
