ID   LIGB_YERPG              Reviewed;         567 AA.
AC   A9R666;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=YpAngola_A0046;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABX87376.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000901; ABX87376.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041854750.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R666; -.
DR   SMR; A9R666; -.
DR   KEGG; ypg:YpAngola_A0046; -.
DR   PATRIC; fig|349746.12.peg.989; -.
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   CDD; cd00114; LIGANc; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_01587; DNA_ligase_B; 1.
DR   InterPro; IPR020923; DNA_ligase_B.
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.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Ligase; NAD.
FT   CHAIN           1..567
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000381953"
FT   ACT_SITE        132
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   567 AA;  63685 MW;  BF92EE0CBCEC9283 CRC64;
     MNILNLKIIM FLLISNTIVV GGAWATSTCP DWPATRIAVE INALEQQLNK WSAAYHQQGH
     SPVTDDIYDQ LQDKLRVWQS CRGLPDKTES QPIPGKGQFL HPVAHTGLKK LKDETALTRW
     MAGRKNLWVQ PKVDGVAVTL VYHGGKLVQL LSRGNGVKGQ NWTEKAPFIS AIPQYIANAP
     ALLTLQGELF LLMDGHQQAK SGGVNARSTV AGALMRKSPS PLLAQVGVFI WAWPDGPTTM
     KEKVALLQVM GFPFTAKYSE PVMSHLDVVQ WRQFWFQAPL PFVTDGVVVR QEEEPAGRYW
     QATPGQWSMA WKYPPLQHIA EVKDIHFTLG RTGKGTVVLE VLPIKIDDKW IRRVNIGSVT
     RWKQWDIAPG DHITLALAGH GIPRLDNVVW RVHQRNTITA PNWDKFHQLS CFQRLPHGCE
     PQFLSRLIWL SGPGGLDIGG IGGGFWQELI HHELINDLVG WLLLTPEQIA SIPGIGNARA
     EKIYQQFQRA KQQPFSRWLL ALGFPQVVSV DAQWQVVLRR SLSEWATMAG IGQMRAKQIK
     HFWDHPDVQA LADFLSTQKV VGFELTE