ID A0A0L0H136_9ENTR Unreviewed; 560 AA.
AC A0A0L0H136;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:KNC95160.1};
GN ORFNames=GM31_06855 {ECO:0000313|EMBL:KNC95160.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC95160.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC95160.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC95160.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC95160.1}.
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DR EMBL; JNGI01000016; KNC95160.1; -; Genomic_DNA.
DR RefSeq; WP_049855995.1; NZ_JNGI01000016.1.
DR AlphaFoldDB; A0A0L0H136; -.
DR STRING; 379893.GCA_001297775_00258; -.
DR PATRIC; fig|379893.4.peg.1401; -.
DR OrthoDB; 9759736at2; -.
DR Proteomes; UP000037393; 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; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01587};
KW DNA repair {ECO:0000256|HAMAP-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 Reference proteome {ECO:0000313|Proteomes:UP000037393};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..560
FT /note="DNA ligase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005539571"
FT DOMAIN 27..424
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT ACT_SITE 123
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01587"
SQ SEQUENCE 560 AA; 61958 MW; 79ED7951E9D9D924 CRC64;
MAKWGWLLVL MVCGSVSAAC PVWPTARADE EIARLSEQIT QWNDAYWTQG VSGANDAVYD
QLSARLAQWR RCFGKDTSAE LAPPMLTKGL VHPVAHTGVK KLPDAAALSG WMKGKSDLWL
QPKVDGVAVT LVYREGKLAQ AISRGDGLKG EDWTARVRLI PAVPQTVSGA LANSVLQGEL
FLRRNGHIQK QMGGMNARAK VAGAMMRKST PESLQALSLF VWAWPDGPKS MSQRLALLRD
AGFDWVSQYS LPVTTAMQVE AQRARWFNSP LPFVTDGIVV REASEPSGKH WLPGQARWIV
AWKYPPVAQV AEVKAVNFAV GRTGKIAVVA QLDPIQLDDK RVQRVNIGSV NRWQQLDLAP
GDQVQVSLAG QGIPRIDSVV WRSAERHKPE PPAGRFTPLT CYFSSPECEA QFLSRLVWSS
SSQALDIDGI GAATWQTLHR THHFSHLFSW LVLTQEQLQA TPGLGTARGL QLWHRFNLAR
NQPFRRWITA MGIPLSQETL NSIAGVNWQQ LLAKSEAEWQ ALPGTGAQRA TRIRQWLNSD
AVSLLAKWLS EQKIDGFSVQ
//
