ID   LIGB_ECO8A              Reviewed;         560 AA.
AC   B7M4D2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=ECIAI1_3818;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928160; CAR00615.1; -; Genomic_DNA.
DR   RefSeq; WP_001384873.1; NC_011741.1.
DR   AlphaFoldDB; B7M4D2; -.
DR   SMR; B7M4D2; -.
DR   KEGG; ecr:ECIAI1_3818; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
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_1000147722"
FT   ACT_SITE        124
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   560 AA;  63211 MW;  B6679B9FE49C8163 CRC64;
     MKVWMAILIS ILCWQSSVWA VCPAWSPARA QEEISRLQQQ IKQWDDDYWK EGKSEVEDGV
     YDQLSARLTQ WQRCFGSEPR DVMMPPLNGA VMHPVAHTGV RKMVDKNALS LWMRERSDLW
     VQPKVDGVAV TLVYRDGKLN KAISRGNGLK GEDWTQKVSL ISAVPQTVSG PLANSTLQGE
     IFLQREGHIQ QQMGGINARA KVAGLMMRQD DSDTLNSLGV FVWAWPDGPQ LMSDRLKELA
     TAGFTLTQTY TRAVKNADEV ARVRNEWWKA ELPFVTDGVV VRGAKEPESR HWLPGQAEWL
     VAWKYQPVAQ VAEVKAIQFA VGKSGKISVV ASLAPVMLDD KKVQRVNIGS VRRWQEWDIA
     PGDQILVSLA GQGIPRIDDV VWRGAERTKP TPPENRFNSL TCYFASDVCQ EQFISRLVWL
     GSKQVLGLDG IGEAGWRALH QTHRFEHIFS WLLLTPEQLQ NTPGIAKSKS AQLWHQFNLA
     RKQPFTRWVM AMGIPLTRAA LNASDERSWS QLLFSTEQFW QQLPGTGSGR ARQVIEWKEN
     AQIKKLGSWL AAQQITGFEP