ID   A7H619_CAMJD            Unreviewed;       282 AA.
AC   A7H619;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=DNA ligase, ATP-dependent {ECO:0000313|EMBL:ABS44161.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:ABS44161.1};
GN   OrderedLocusNames=JJD26997_2043 {ECO:0000313|EMBL:ABS44161.1};
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109 {ECO:0000313|EMBL:ABS44161.1, ECO:0000313|Proteomes:UP000002302};
RN   [1] {ECO:0000313|Proteomes:UP000002302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97
RC   {ECO:0000313|Proteomes:UP000002302};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034003};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR   EMBL; CP000768; ABS44161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H619; -.
DR   KEGG; cjd:JJD26997_2043; -.
DR   HOGENOM; CLU_021047_0_0_7; -.
DR   Proteomes; UP000002302; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR   CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR   Gene3D; 3.30.1490.70; -; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR029319; DNA_ligase_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR47810; DNA LIGASE; 1.
DR   PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF14743; DNA_ligase_OB_2; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:ABS44161.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..282
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012474726"
FT   DOMAIN          108..200
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   282 AA;  32530 MW;  AC8A84C05825A0A7 CRC64;
     MRFIFLICCA CLVFANEILL LSKFDKQDFN SKDFNAYLMS EKLDGVRGIW DGKYLKTRQN
     YKIKTPDFFT KNFPPFAIDG ELWIARNKFD EISALIRSGD SNLTLWKEVT YNIFDVPNAC
     EEFQISTCTL KNRLAVLEEY LQKYPSAYIK IIPQIPVENQ NNLNQFYESI IKNQGEGIVI
     RKNLSPYEKG RSKNAMKLKP YDDAECELVG FRKGKGKFEN QVGALLCKMP NGQIIKIGSG
     LKDKDRKNPP KIGSIITYKF NGLTKNSLPR FPVFLRIRDE NP
//