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LIGB_SALPC
ID   LIGB_SALPC              Reviewed;         561 AA.
AC   C0Q1X9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=SPC_3821;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(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; CP000857; ACN47895.1; -; Genomic_DNA.
DR   RefSeq; WP_001241849.1; NC_012125.1.
DR   AlphaFoldDB; C0Q1X9; -.
DR   SMR; C0Q1X9; -.
DR   EnsemblBacteria; ACN47895; ACN47895; SPC_3821.
DR   KEGG; sei:SPC_3821; -.
DR   HOGENOM; CLU_489786_0_0_6; -.
DR   OMA; DLWIQPK; -.
DR   Proteomes; UP000001599; 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_1000185681"
FT   ACT_SITE        125
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ   SEQUENCE   561 AA;  62855 MW;  B725FBB165387CE0 CRC64;
     MRLWKSMAWG ILLWHSQSGA LCPAWPPARA AEEITRLQQQ LADWNDIYWK QGVSAVDDSV
     YDQLSARLVQ WQRCVGQDVS STPVSPPLNG TTMHPVAHTG VRKLADRQAV EQWMRGRSEL
     WVQPKVDGVA VTLVYQNGKL TRAISRGNGL QGEDWTPKIR LIPSIPQTTQ GALANAVLQG
     EIFLQREGHI QQRMGGMNAR SKVAGMLMRQ DNASALNSLG IFIWAWPDGP ANMPERLSQL
     AKAGFSLTNK YTLAVKDASE VERARQSWLT SALPFVTDGV VIRMAKEPAS QHWRPGQGDW
     LAAWKYPPVA QVAQVSAIQF SVGKSGKITV VASLVPVILD DKRVQRVNIG SVKRWEAWDI
     APGDQILVSL AGQGIPRLDE VVWRSRERSK PVPPDSHFNS LTCFYASATC QEQFISRLVW
     LGSRSALGLD GMGEASWRAL HQTHRFEHIF SWLALTSAQI ANTPGFAKGK SEQIWRQFNL
     ARRQPFTRWI MAMDIPLTQA ALQASGDRSW EQLLMRTEQH WRQLPATGER RAGRVIDWRD
     NPQIKTLSRW LAAQHIPGFG S
 
 
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