ID   LIGB_KLEP7              Reviewed;         564 AA.
AC   A6TFP6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=KPN78578_39560; ORFNames=KPN_03995;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR79380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6TFP6; -.
DR   SMR; A6TFP6; -.
DR   STRING; 272620.KPN_03995; -.
DR   EnsemblBacteria; ABR79380; ABR79380; KPN_03995.
DR   KEGG; kpn:KPN_03995; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   Proteomes; UP000000265; 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; 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; Reference proteome.
FT   CHAIN           1..564
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000313542"
FT   ACT_SITE        130
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   564 AA;  63311 MW;  591B431DEC9B29B4 CRC64;
     MEEGTAMRKG GWWLALGMFS ASALATCPDW PLARGRQETS RLHQQIVAWK EAYWRQGASG
     VSDDVYDQLT LRLAQWRQCF PGATPEDDDL PPPTGDARHP VAHTGVRKLA DEDSVARWMK
     NKSDLWIQPK VDGVAVTLVY RQGRLVQAIS RGDGLRGEAW TARARQIPAL AKVMTGELAD
     SVLQGELFLR RDGHVQQQTG GMNARAKVAG LMMRADAAAA LSQLDVFIWA WPDGPSDMRR
     RQQLLAQAGF KYSGQYTHPV SRIEQVAQWR QRWYRSPLPF VSDGVIVREG REPPGRVWSP
     GKGEWLAAWK YPPASRVMQV RAIRFSIGRS GRLNVVAELE PQRLDDKRVQ RVNVGSVSRW
     QMLDIGVGDQ LQISLAGQGI PRVDAVVWRT AERHKPTPPP AKFNALTCYF ATPECSEQFL
     SRLIWLSSKS ALNVDGVGEN LWRVIQQQNP MTHIFSWLAL TVEQLQAVPG ISAARGQHLW
     HQFDLVRKRP FIRWVLAMGI PVPQGALAQL ESENWHLLAA KSEAQWRTLP GVGEIRARQL
     VAFLHHPDVV ALAQWLSGQR IPGF