ID   LIGB_ECO5E              Reviewed;         560 AA.
AC   B5YWE6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
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};
GN   OrderedLocusNames=ECH74115_5017;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACI36824.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001164; ACI36824.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001303719.1; NC_011353.1.
DR   AlphaFoldDB; B5YWE6; -.
DR   SMR; B5YWE6; -.
DR   KEGG; ecf:ECH74115_5017; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
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..560
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000381948"
FT   ACT_SITE        124
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   560 AA;  63381 MW;  1EEC2659B78F462F CRC64;
     MKVWMAILIS ILCWQSSVWA VCPAWSPARA QEEIFRLQQQ IKQWDDDYWK EGKSEVEDGV
     YDQLSARLTQ WQRCFVSEPR DVMMPPLNGA VMHPVAHTGV RKMADKNALS LWMRERSDLW
     VQPKVDGVAV TLVYRDGKLN KAISRGNGLK GEDWTQKVSL ISAVPQTVSG PLANSTLQGE
     IFLQREGHIQ QQMGGINARA KVAGLMMRQD DSDTLNSLGV FVWAWPDGPQ LMTDRLKELA
     TAGFTLTQRY TRAVKNADEV ARVRNEWWKA KLPFVTDGVV VRGAKEPESR HWLPGQAEWL
     VAWKYQPVAQ VAKVKAIQFA VGKSGKISVV ASLAPVMLDD KKVQRVNIGS VRRWQEWDIA
     PGDQILVSLA GQGIPRIDDV VWRGAERTKP TPPENRFNSL TCYFASDVCQ EQFISRLVWL
     GSKQVLGLDG IGEAGWRALH QTHRFEHIFS WLLLTPEQLQ NTPGIAKSKS AQLWHRFNLA
     RKQPFTRWVM AMGIPLTRAA LNASDERSWS QLLFSTEQFW QQLPGTGSGR ARQVIEWKEN
     AQIKKLGSWL AAQQITGFEP