ID   LIGB_ECOLU              Reviewed;         560 AA.
AC   B7NEV1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=ECUMN_4162;
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR15303.1; -; Genomic_DNA.
DR   RefSeq; WP_001309848.1; NC_011751.1.
DR   RefSeq; YP_002414800.1; NC_011751.1.
DR   AlphaFoldDB; B7NEV1; -.
DR   SMR; B7NEV1; -.
DR   STRING; 585056.ECUMN_4162; -.
DR   EnsemblBacteria; CAR15303; CAR15303; ECUMN_4162.
DR   KEGG; eum:ECUMN_4162; -.
DR   PATRIC; fig|585056.7.peg.4336; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   Proteomes; UP000007097; 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..560
FT                   /note="DNA ligase B"
FT                   /id="PRO_1000147724"
FT   ACT_SITE        124
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   560 AA;  63142 MW;  496D2BABBA0DB2CF CRC64;
     MKVWMAILIS ILCWQSSAWA VCPAWSPARA QEEISRLQQQ IKQWDDDYWK EGKSEVEDGV
     YDQLSARLTQ WQRCFGNETP DVMMPPLNGA VIHPVAHTGV RKMADKIALS LWMRERSDLW
     VQPKVDGVAV TLVYRDGKLN KAISRGNGLK GEDWTQKVRL ISAVPQTVSG PLANSTLQGE
     IFLKREGHIQ QQMGGINARA KVAGLMMRQD DSDTLNSLGV FVWAWPDGPQ LMTDRLKELA
     TAGFTLTQTY TRAVKNADEV ARVRNAWWKA KLPFVTDGVV VRAAKEPESR HWLPGQAEWL
     VAWKYQPVAQ VAEVKTIQFA VGKSGKISVV ASLAPVMLDD KKVQRVNIGS VRRWQEWDIA
     PGDQILVSLA GQGIPRIDDV VWRGAERTKP TPPENRFNSL TCYFASDVCQ EQFISRLVWL
     GSKQVLGLDG IGEAGWRALH QTHRFEHIFS WLLLTPEQLQ NTPGIAKSKS AQLWHQFNLA
     RKQPFTRWVM AMGIPLTRAA LNASDERSWS QLLLSTEQFW QQLPGTGSGR ARQVIEWKEN
     AQIKKLGSWL AAQQITGFEP