LIGB_ECO7I
ID LIGB_ECO7I Reviewed; 560 AA.
AC B7NQ11;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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};
GN OrderedLocusNames=ECIAI39_4168;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928164; CAR20276.1; -; Genomic_DNA.
DR RefSeq; WP_012602584.1; NC_011750.1.
DR RefSeq; YP_002410045.1; NC_011750.1.
DR AlphaFoldDB; B7NQ11; -.
DR SMR; B7NQ11; -.
DR STRING; 585057.ECIAI39_4168; -.
DR EnsemblBacteria; CAR20276; CAR20276; ECIAI39_4168.
DR KEGG; ect:ECIAI39_4168; -.
DR PATRIC; fig|585057.6.peg.4318; -.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR Proteomes; UP000000749; 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_1000147721"
FT ACT_SITE 124
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 560 AA; 63198 MW; 51B0CB53DB0F05AA CRC64;
MKVWMAILIS ILCWQSSAWA VCPAWSPARA QEEISRLQQQ IKQWDDDYWK EGKSEVEDGV
YDQLSARLTQ WQRCFGNETR DAMMPPLNGA VMHPVAHTGV RKMADKNALS LWMRERSDLW
VQPKVDGVAV TLVYRDGKLN KAISRGNGLK GEDWTQKVRL ISAVPQTVSG PLANSTLQGE
IFLKRKGHIQ QQMGGINARA KVAGLMMRQG NSDTLNSLAV FVWAWPDGPQ LMTDRLKELA
TAGFTLTQTY TRAVKNADEV AHVRNEWWKA KLPFVTDGVV VRAAKEPESR HWLPGQAEWL
VAWKYQPVAQ VAEVKAIQFA VGKSGKISVV ASLVPVMLDD KKVQRVNIGS VRHWQEWDIA
PGDQILVSLA GQGIPRIDDV VWRGAERTKP TPPENRFNSL TCYFASDVCQ EQFISRLVWL
GSKQVLGLDG IGEAGWRALH QTHRFEHIFS WLLLTPEQLQ NTPGIAKSKS AQLWHQFNLA
RQQPFTRWVM AMGIPLTRAA LNASDERSWS QLLFSTEQFW QQLPGTGSGR ARQVIEWKEN
AQIKKLGSWL AAQQITGFEP