ID   LIGB_SALDC              Reviewed;         561 AA.
AC   B5FM71;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=DNA ligase B {ECO:0000255|HAMAP-Rule:MF_01587};
DE            EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01587};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B {ECO:0000255|HAMAP-Rule:MF_01587};
GN   Name=ligB {ECO:0000255|HAMAP-Rule:MF_01587}; OrderedLocusNames=SeD_A4126;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Catalyzes the formation of phosphodiester linkages between
CC       5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD
CC       as a coenzyme and as the energy source for the reaction.
CC       {ECO:0000255|HAMAP-Rule:MF_01587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01587};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01587}.
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DR   EMBL; CP001144; ACH76115.1; -; Genomic_DNA.
DR   RefSeq; WP_001241843.1; NC_011205.1.
DR   AlphaFoldDB; B5FM71; -.
DR   SMR; B5FM71; -.
DR   KEGG; sed:SeD_A4126; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   Proteomes; UP000008322; Chromosome.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_01587; DNA_ligase_B; 1.
DR   InterPro; IPR018239; DNA_ligase_AS.
DR   InterPro; IPR020923; DNA_ligase_B.
DR   InterPro; IPR033136; DNA_ligase_CS.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR   PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Ligase; NAD.
FT   CHAIN           1..561
FT                   /note="DNA ligase B"
FT                   /id="PRO_1000147727"
FT   ACT_SITE        125
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   561 AA;  62911 MW;  F5D9F446B1BC70DE CRC64;
     MRLWKSMAWG ILLWHSQSGA LCPAWPPARA AEEITRLQQQ LADWNDIYWK QGVSAVDDSV
     YDQLSARLVQ WQRCVGQDVS STPVSPPLNG TTMHPVAHTG VRKLADRQAV EQWMRGRSEL
     WVQPKVDGVA VTLVYQNGKL TRAISRGNGL QGEDWTPKIR LIPSIPQTTQ GALANAVLQG
     EIFLQREGHI QQRMGGMNAR SKAAGMLMRQ DNASALNSLG IFIWAWPDGP ANMPERLSQL
     AKAGFSLTKK YSLAVKDASE VERARQSWLT SALPFVTDGV VIRMAKEPAS QYWRPGQGDW
     LAAWKYPPVA QVAQVSAIQF SVGKSGKITV VASLVPVILD DKRVQRVNIG SVKRWEAWDI
     APGDQILVSL AGQGIPRLDE VVWRSRERSK PVPPDSHFNS LTCFYASETC QEQFISRLVW
     LGSRSALGLD GMGEASWRAL HQTHRFEHIF SWLALTSAQI ANTPGFAKGK SEQIWRQFNL
     ARRQPFTRWI MAMDIPLTQA ALQASGDRSW EQLLMRTEQH WRQLPATGER RAGRVIDWRD
     NPQIKTLSRW LAAQHIPGFG S