LIGB_SALA4
ID LIGB_SALA4 Reviewed; 561 AA.
AC B5EXF2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=SeAg_B3956;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(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}.
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DR EMBL; CP001138; ACH48897.1; -; Genomic_DNA.
DR RefSeq; WP_001241833.1; NC_011149.1.
DR AlphaFoldDB; B5EXF2; -.
DR SMR; B5EXF2; -.
DR EnsemblBacteria; ACH48897; ACH48897; SeAg_B3956.
DR KEGG; sea:SeAg_B3956; -.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR Proteomes; UP000008819; 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_1000147726"
FT ACT_SITE 125
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 561 AA; 62898 MW; 3C7D9D6E046B2477 CRC64;
MRLWKSMAWG ILLWHSQSGA LCPAWPPARA AEEIARLQQQ LADWNDIYWK QGVSAVDDSV
YDQLSARLVQ WQRCVGQDVS STPVSPPLNG TTMHPVAHTG VRKLADRQAV EQWMRGRSEL
WVQPKVDGVA VTLVYQNGKL TRAISRGNGL QGEDWTPKIR LIPSIPQTTQ GALANAVLQG
EIFLQREGHI QQRMGGMNAR SKVAGMLMRQ DNASALNSLG IFIWAWPDGP ANMPERLSQL
AKAGFSLTKK YSLVVKDASE VERARQSWLT SALPFVTDGV VIRMAKEPAS QYWRPGQGDW
LAAWKYPPVA QVAQVSAIQF SVGKSGKITV VASLVPVILD DKRVQRVNIG SVKRWEAWDI
APGDQILVSL AGQGIPRLDE VVWRSRERSK PVPPDSHFNS LTCFYASATC QEQFISRLVW
LGSRSALGLD GMGEASWRAL HQTHRFEHIF SWLTLTSAQI ANTPGFAKGK SEQIWRQFNL
ARRQSFTRWI MAMDIPLTQA ALQASGDRSW EQLLMRTEQH WRQLPATGER RAGRVIDWRN
NPQIKTLSRW LAAQHIPGFG S