ID A0A0T9WHF2_SALET Unreviewed; 561 AA.
AC A0A0T9WHF2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=DNA ligase B {ECO:0000256|HAMAP-Rule:MF_01587};
DE EC=6.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01587};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B {ECO:0000256|HAMAP-Rule:MF_01587};
GN Name=ligB {ECO:0000256|HAMAP-Rule:MF_01587,
GN ECO:0000313|EMBL:SUE45442.1};
GN ORFNames=B7N00_13415 {ECO:0000313|EMBL:EDG5017946.1}, B7N35_02495
GN {ECO:0000313|EMBL:EDG5124899.1}, B7N72_08360
GN {ECO:0000313|EMBL:EDG5370118.1}, B7N78_05520
GN {ECO:0000313|EMBL:EDG5279235.1}, B7N84_10960
GN {ECO:0000313|EMBL:EDG5266853.1}, DRU31_06270
GN {ECO:0000313|EMBL:EBS2451932.1}, E0916_11410
GN {ECO:0000313|EMBL:ECF1446556.1}, ERS008207_00604
GN {ECO:0000313|EMBL:CNT68824.1}, EWC73_01935
GN {ECO:0000313|EMBL:ECE8534987.1}, G0B02_03005
GN {ECO:0000313|EMBL:HAC6378104.1}, G0D18_06335
GN {ECO:0000313|EMBL:HAC6680283.1}, G2206_12395
GN {ECO:0000313|EMBL:HAE0435558.1}, NCTC5754_00212
GN {ECO:0000313|EMBL:SUE45442.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE45442.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|EMBL:CNT68824.1, ECO:0000313|Proteomes:UP000042394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D4891 {ECO:0000313|EMBL:CNT68824.1,
RC ECO:0000313|Proteomes:UP000042394};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6378104.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378104.1}, M123
RC {ECO:0000313|EMBL:HAC6680283.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435558.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE45442.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE45442.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EBS2451932.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=143652 {ECO:0000313|EMBL:EDG5370118.1}, 273631
RC {ECO:0000313|EMBL:EDG5017946.1}, 330535
RC {ECO:0000313|EMBL:EDG5266853.1}, 333944
RC {ECO:0000313|EMBL:EDG5279235.1}, 337042
RC {ECO:0000313|EMBL:EDG5124899.1}, 387147
RC {ECO:0000313|EMBL:EBS2451932.1}, 470200
RC {ECO:0000313|EMBL:ECE8534987.1}, and 692616
RC {ECO:0000313|EMBL:ECF1446556.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAC6680283.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378104.1}, M123
RC {ECO:0000313|EMBL:HAC6680283.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435558.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00034005, ECO:0000256|HAMAP-
CC Rule:MF_01587};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01587}.
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DR EMBL; CQPD01000004; CNT68824.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000004; EBS2451932.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000002; ECE8534987.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000006; ECF1446556.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000008; EDG5017946.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000002; EDG5124899.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000005; EDG5266853.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000003; EDG5279235.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000006; EDG5370118.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000002; HAC6378104.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000004; HAC6680283.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000012; HAE0435558.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE45442.1; -; Genomic_DNA.
DR RefSeq; WP_001241840.1; NZ_WFIN01000005.1.
DR AlphaFoldDB; A0A0T9WHF2; -.
DR Proteomes; UP000042394; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01587};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01587};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01587};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..561
FT /note="DNA ligase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015046567"
FT DOMAIN 29..426
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT ACT_SITE 125
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01587"
SQ SEQUENCE 561 AA; 62894 MW; 620B38BACDC6EBB0 CRC64;
MRLWKSMAWG ILLWHSQSGA LCPAWPPARA AEEITRLQQQ LADWNDIYWK QGVSAVDDSV
YDQLSARLVQ WQRCVGQDVS STPVSPPLNG TTMHPVAHTG VRKLADRQAV EQWMRGRSEL
WVQPKVDGVA VTLVYQNGKL ARAISRGNGL QGEDWTPKIR LIPSIPQSTQ GALANAVLQG
EIFLQREGHI QQRMGGMNAR SKVAGMLMRQ DNASALNSLG IFIWAWPDGP ANMPERLSQL
AKAGFSLTKK YSLVVKDASE VERARQSWLT SALPFVTDGV VIRMAKEPAS QYWRPGQGDW
LAAWKYPPVA QVAQVSAIQF SVGKSGKITV VASLVPVILD DKRVQRVNIG SVKRWEAWDI
APGDQILVSL AGQGIPRLDE VVWRSRERSK PVPPDSHFNS LTCFYASATC QEQFISRLIW
LGSRSALGLD GMGEASWRAL HQTHRFEHIF SWLTLTSAQI ANTPGFAKGK SEQIWRQFNL
ARRQPFTRWI MAMDIPLTQA ALQASGDRSW EQLLMRTEQH WRQLPATGER RAGRVIDWRN
NLQIKALSRW LAAQHIPGFG S
//
