ID   LIGB_CROS8              Reviewed;         561 AA.
AC   A7MQB5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=ESA_04079;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU79260.1; -; Genomic_DNA.
DR   RefSeq; WP_012126235.1; NC_009778.1.
DR   AlphaFoldDB; A7MQB5; -.
DR   SMR; A7MQB5; -.
DR   EnsemblBacteria; ABU79260; ABU79260; ESA_04079.
DR   KEGG; esa:ESA_04079; -.
DR   PATRIC; fig|290339.8.peg.3624; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   OrthoDB; 241401at2; -.
DR   Proteomes; UP000000260; 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..561
FT                   /note="DNA ligase B"
FT                   /id="PRO_0000313535"
FT   ACT_SITE        124
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   561 AA;  62771 MW;  3AA7FB384F56461E CRC64;
     MRITIFLLLI ILASAGAYAA CPDWTPQQAQ QEVAALENQL TRWDEAYWLH GENKVSDAVY
     DSMRQRLRAW QTCFALPVFN DAPVALAAGR TRHPVAHTGV QKLNDATSLS QWMHGKTDLW
     VQPKVDGVAV SLVYRKGKLQ QVISRGDGER GEDWTARARH IPAIPLQVTG ELADSVLQGE
     LFLRQTGHRQ QQDGGINARG QVAGAMMRST VSSVLNDLDL FIWAWPDGPK AMEARLSTLA
     EGGFPLAQAW SKPVHSVSDV ARLREQWFSE PLPFVTDGVV IREGREPPGK SWRPGEGSWV
     VAWKYPPAKQ ITEIKALRFA VGRTGKISVV AQLEPVTLDD KKVSKVSIGS LARWEKLDLA
     EGDQVEISLA GQGIPRLDAV IWRPTQRIKP VPPTARFDTL SCLYGTTGCE EQFISRLVWL
     SGKHVFDLAG MGEATWRQLS EHHHFEHLFS WLALSVDALK QTPGFSAQRA AQLWHQFNLT
     RQQPFQRWVK ALGLPLPARD WQALTDDKWQ QLQARDERSW QTLPGVGAER ARQLVSYIHH
     PDIAALAEWL AAQRIDGFAL P