ID   G0AQ70_9GAMM            Unreviewed;       309 AA.
AC   G0AQ70;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=DNA ligase (ATP) {ECO:0000313|EMBL:AEG11752.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:AEG11752.1};
DE   Flags: Precursor;
GN   ORFNames=Sbal175_2501 {ECO:0000313|EMBL:AEG11752.1};
OS   Shewanella baltica BA175.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG11752.1, ECO:0000313|Proteomes:UP000002249};
RN   [1] {ECO:0000313|EMBL:AEG11752.1, ECO:0000313|Proteomes:UP000002249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA175 {ECO:0000313|EMBL:AEG11752.1,
RC   ECO:0000313|Proteomes:UP000002249};
RX   PubMed=22328742; DOI=10.1128/JB.06468-11;
RA   Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA   Konstantinidis K.T.;
RT   "Genome sequencing of five Shewanella baltica strains recovered from the
RT   oxic-anoxic interface of the Baltic Sea.";
RL   J. Bacteriol. 194:1236-1236(2012).
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; CP002767; AEG11752.1; -; Genomic_DNA.
DR   RefSeq; WP_006081348.1; NC_017571.1.
DR   AlphaFoldDB; G0AQ70; -.
DR   KEGG; sbb:Sbal175_2501; -.
DR   HOGENOM; CLU_021047_0_0_6; -.
DR   Proteomes; UP000002249; 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; 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.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:AEG11752.1}.
FT   DOMAIN          98..220
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          234..299
FT                   /note="DNA ligase OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF14743"
SQ   SEQUENCE   309 AA;  34903 MW;  C3F31AD629ED35F0 CRC64;
     MTHTSPLQDL TFHRFIRFRF FKQRLLLLSL LIFGCLAPVT YAQNSPPSIQ LATEFDAQQE
     IHIQDFLISE KLDGVRGYWN GQALLTRQGN LIAVPTWFIA NFPNYPLDGE LWLGRGQFEA
     MSSIVRQTSA KDDDWRKVRF MVFDVPKAGG DFQHRYQFAL AELSDKSHYL EVIAQFQVDS
     LEALYQKLDS LVAKGAEGLM LHRSSATYVS GRNPNLMKLK PYYDAEATVI GHIPGKGQFA
     GQMGAIRVQT PDGRIFNIGT GFNLAERQHP PAVGAIITYK YLGLTVNGLP RFASFLRVRV
     DIDKIDSQQ
//