LIGB_ECOL5
ID LIGB_ECOL5 Reviewed; 560 AA.
AC Q0TBG2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 83.
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=ECP_3745;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABG71717.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000247; ABG71717.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001541786.1; NC_008253.1.
DR AlphaFoldDB; Q0TBG2; -.
DR SMR; Q0TBG2; -.
DR STRING; 362663.ECP_3745; -.
DR EnsemblBacteria; ABG71717; ABG71717; ECP_3745.
DR KEGG; ecp:ECP_3745; -.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR Proteomes; UP000009182; 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..560
FT /note="DNA ligase B"
FT /id="PRO_0000313541"
FT ACT_SITE 124
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 560 AA; 63172 MW; BCA42BE7C6CDEF03 CRC64;
MKVWMAILIS ILCWQSSAWA VCPAWSPARA QEEISRLQQQ IKQWDDDYWK EGESEIEDGV
YDQLSARLTQ WQRCFGNEPR DAMMPPLAGT VMHPVAHTGV RKLADKNALR LWMREHNDLW
VQPKVDGVAV TLVYRDGKLN KAISRGNGLK GEDWTQKVSL ISAVPQTVSG PLANSTLQGE
IFLKRKGHIQ QQMGGINARA KVAGLMMRQG NSDTLNSLAV FVWAWPDGPH LMTDRLKDLA
TAGFTLTQTY TRAVKNADEV AHVRNEWWKA KLPFVTDGVV VRAAKEPESR HWLPGQAEWL
VAWKYQPVAQ VAEVKAIQFA VGKSGKISVV ASLAPVMLDD KKVQRVNIGS VRRWQEWDIA
PGDQILVSLA GQGIPRIDDV VWRGAERTKP TPPENRFNSL TCYFASDVCQ EQFISRLVWL
GSKQVLGLDG IGEAGWRALH QTHRFEHIFS WLLLTPEQLQ NTPGIAKSKS AQLWHQFNLA
RQQPFTRWVM AMGIPLTRAA LNASDERSWS QLLFSTEQFW QQLPGTGSGR ARQVIEWKEN
AQIKKLGSWL AAQQITGFEP