ID   LIGB_KLEP3              Reviewed;         558 AA.
AC   B5XTF0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=KPK_0101;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI07377.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XTF0; -.
DR   SMR; B5XTF0; -.
DR   EnsemblBacteria; ACI07377; ACI07377; KPK_0101.
DR   KEGG; kpe:KPK_0101; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   OrthoDB; 241401at2; -.
DR   Proteomes; UP000001734; 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.
FT   CHAIN           1..558
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000381949"
FT   ACT_SITE        124
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   558 AA;  62517 MW;  1062494CD36E87AD CRC64;
     MRKGGWWLAL GMFSASALAT CPDWPPARGR QEISRLHQQI VAWKEDYWRQ GASEVSDEVY
     DQLTLRLAQW RQCFPGTTPE DDDLPPPTGD ARHPVAHTGV RKLADEVSVA HWMKNKTDLW
     IQPKVDGVAV TLVYRQGSLV QAISRGDGLR GEAWTARARQ IPALAKVTTG ELANSVLQGE
     LFLRRDGHVQ QQAGGMNARA KVAGLMMRAD AAAALSQLDV FIWAWPDGPS DMRRRQQLLT
     QAGFKYSGQY THPVTRVEQV AQWRQRWYRS PLPFVSDGVI VREGREPPGR AWSPGKGEWL
     AAWKYPPASQ VMEVRAIHFS TGRSGRLNVV AQLEPQRLDD KRVQRVNVGS VARWQALDIG
     VGDQLQISLA GQGIPRIDAV VWRTAERHKP TPPAAKFNAL TCYFATPECS EQFLSRLIWL
     SSKSALDVDG VGEHLWRAIQ QQNPMTHIFS WLALTVEQLQ AVPGISAARG QHLWHQFDLV
     RKRPFIRWVL AMGLPVPQGA LAQLESENWH LLAAKSEAQW RALPGVGEIR ARQLVAFLHH
     PDVVALAQWL SGQRIPGF