ID A0A077L9X2_9PSED Unreviewed; 566 AA.
AC A0A077L9X2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=PSCI_0468 {ECO:0000313|EMBL:BAP41170.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP41170.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP41170.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP41170.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
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};
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DR EMBL; AP014637; BAP41170.1; -; Genomic_DNA.
DR RefSeq; WP_045482346.1; NZ_AP014637.1.
DR AlphaFoldDB; A0A077L9X2; -.
DR STRING; 1028989.PSCI_0468; -.
DR KEGG; pses:PSCI_0468; -.
DR HOGENOM; CLU_005138_6_2_6; -.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000031652; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA 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:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07897; Adenylation_DNA_ligase_Bac1; 1.
DR CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 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; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR04120; DNA_lig_bact; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:BAP41170.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031652}.
FT DOMAIN 339..467
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 566 AA; 63462 MW; F480A77290F83E99 CRC64;
MKAFAELYAR LDATTSSNAK LAALHDYFAQ APAEDAAWAV YFLAGGRPRQ LVPSRVLREQ
ATALSDLPPW LFEESYQAVG DLAETLSLLL PHAEHSNDEG LAVWLEQHLL PLRGLPPEEL
AERLPALWAQ LDRNSLMVCI KLITGSFRVG VSKLLVTRAL AALTGLDSKR IAQRLVGYTD
LSHRPGAQAY LKLIAPESDD EHAQRGGQPY PFFLAHALQQ PVEQFETLLG PAQDWLVEWK
WDGIRAQLVK RDGQLWVWSR GEELMTERFP ELHSLAQILP DGTVIDGEIV VWKAAETPAD
ETKDFALSGE PDNAPWVQPF ALLQQRIGRK TLGKKLLGDA PVVLLGYDLL EWQGEDWRSH
PQHQRRAQLD QLIEASQSPV LLPSPVLSGQ NWKALAELRE DARRLGVEGM MLKARESLYG
VGRTKDMGVW WKWKLDPFSV DAVLIYAQRG HGRRASLYSD YTFAVWDSPP GSSERTLVPF
AKAYSGLTDE EMRKVDAIIR KTTVEKFGPV RSVTPTLVFE LGFEGIALSK RHKSGIAVRF
PRMLRWRQDK PVDEADSLAT LQDLLG
//