ID   B1I0K1_LYSSC            Unreviewed;       282 AA.
AC   B1I0K1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Putative DNA ligase-like protein {ECO:0000313|EMBL:ACA42360.1};
GN   OrderedLocusNames=Bsph_p130 {ECO:0000313|EMBL:ACA42360.1};
OS   Lysinibacillus sphaericus (strain C3-41).
OG   Plasmid pBsph {ECO:0000313|EMBL:ACA42360.1,
OG   ECO:0000313|Proteomes:UP000002164}.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA42360.1, ECO:0000313|Proteomes:UP000002164};
RN   [1] {ECO:0000313|EMBL:ACA42360.1, ECO:0000313|Proteomes:UP000002164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41 {ECO:0000313|EMBL:ACA42360.1,
RC   ECO:0000313|Proteomes:UP000002164};
RC   PLASMID=pBsph {ECO:0000313|EMBL:ACA42360.1,
RC   ECO:0000313|Proteomes:UP000002164};
RX   PubMed=18296527; DOI=10.1128/JB.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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; CP000818; ACA42360.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1I0K1; -.
DR   EnsemblBacteria; ACA42360; ACA42360; Bsph_p130.
DR   KEGG; lsp:Bsph_p130; -.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   Proteomes; UP000002164; Plasmid pBsph.
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:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 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   Ligase {ECO:0000313|EMBL:ACA42360.1};
KW   Plasmid {ECO:0000313|EMBL:ACA42360.1}.
FT   DOMAIN          97..187
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   282 AA;  32454 MW;  0AA6698CE1A008F7 CRC64;
     MLVATGIEII NTEDWLYQVK WDGWRVLIHK AGDRIEAFTR EGNNITAKFP ELEEVGHSIT
     VDTAIIDTEG VVLRQGISVF EDFSYRGILT NKEKIKEATI THPVTFVAFD ILTTDKKLMH
     HPLFERKEHL SSIITPSNSL QVTPSVDGDG SNIFEITKDK GMEGIIGKKR DSIYQLNHRS
     KNWLKYKHFK IIETVILAYR ENPFSILVGT ELESGRYKRL ATVEFGFKPE EKMAFRHIAK
     SVITTVDRDL IWLEPRLYCK VQYLEKTNSG LLRTVSFKGF IF
//