ID   A8ESN9_ALIB4            Unreviewed;       284 AA.
AC   A8ESN9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=ATP-dependent DNA ligase {ECO:0000313|EMBL:ABV66963.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:ABV66963.1};
GN   Name=ligA {ECO:0000313|EMBL:ABV66963.1};
GN   OrderedLocusNames=Abu_0698 {ECO:0000313|EMBL:ABV66963.1};
OS   Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Aliarcobacter.
OX   NCBI_TaxID=367737 {ECO:0000313|EMBL:ABV66963.1, ECO:0000313|Proteomes:UP000001136};
RN   [1] {ECO:0000313|EMBL:ABV66963.1, ECO:0000313|Proteomes:UP000001136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018 {ECO:0000313|EMBL:ABV66963.1,
RC   ECO:0000313|Proteomes:UP000001136};
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA   Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the Epsilonproteobacterium
RT   Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV66963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8ESN9; -.
DR   STRING; 367737.Abu_0698; -.
DR   KEGG; abu:Abu_0698; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_021047_0_0_7; -.
DR   Proteomes; UP000001136; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:ABV66963.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001136};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          140..206
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   284 AA;  33441 MW;  958B2B19E9E4817D CRC64;
     MMFFKNIKNI INLFGGLIMK LLLYFFLAIY GFSFELQKAN IYDEKKDNIN NWYMSEKLDG
     IRAYWNGKEL LSKNGNKIYA PSWFIQNLPP FELDGELYTK VNDFENIQSI VLDTKPSKAW
     EKITYNIFEV PNTKGDFDTR LKRLEDWLKI NPNNFIKIIP QIVCKDKEHL DKFLNQMLKK
     QAEGVMIKNP FLEYQEGRNS NILKVKTFFD EEGVVISHNY KNGKFKSLVI KQKDGITFNL
     GNGFTNKDRE NPPKIGDIVT FKYYGLTKNN KPKFASFLRV RKEE
//