LIGB_ECOLI
ID LIGB_ECOLI Reviewed; 560 AA.
AC P25772; P78120; Q2M7W0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DNA ligase B;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] B;
GN Name=ligB; Synonyms=yicF; OrderedLocusNames=b3647, JW3622;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
RC STRAIN=K12;
RX PubMed=8390989; DOI=10.1016/s0021-9258(19)85243-2;
RA Gentry D., Bengra C., Ikehara K., Cashel M.;
RT "Guanylate kinase of Escherichia coli K-12.";
RL J. Biol. Chem. 268:14316-14321(1993).
RN [5]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF LYS-124.
RC STRAIN=K12;
RX PubMed=11812821; DOI=10.1093/nar/29.24.4930;
RA Sriskanda V., Shuman S.;
RT "A second NAD(+)-dependent DNA ligase (LigB) in Escherichia coli.";
RL Nucleic Acids Res. 29:4930-4934(2001).
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:0000269|PubMed:11812821}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11812821};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11812821};
CC -!- MISCELLANEOUS: Considerably less active in nick joining than LigA.
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62000.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB88710.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L10328; AAA62000.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76671.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77646.1; -; Genomic_DNA.
DR EMBL; M84400; AAB88710.1; ALT_INIT; Genomic_DNA.
DR PIR; A65166; A65166.
DR RefSeq; NP_418104.2; NC_000913.3.
DR RefSeq; WP_000870036.1; NZ_LN832404.1.
DR AlphaFoldDB; P25772; -.
DR SMR; P25772; -.
DR BioGRID; 4262567; 167.
DR IntAct; P25772; 3.
DR STRING; 511145.b3647; -.
DR PaxDb; P25772; -.
DR PRIDE; P25772; -.
DR DNASU; 948164; -.
DR EnsemblBacteria; AAC76671; AAC76671; b3647.
DR EnsemblBacteria; BAE77646; BAE77646; BAE77646.
DR GeneID; 948164; -.
DR KEGG; ecj:JW3622; -.
DR KEGG; eco:b3647; -.
DR PATRIC; fig|511145.12.peg.3767; -.
DR EchoBASE; EB1310; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_489786_0_0_6; -.
DR OMA; DLWIQPK; -.
DR PhylomeDB; P25772; -.
DR BioCyc; EcoCyc:EG11334-MON; -.
DR BioCyc; MetaCyc:EG11334-MON; -.
DR PRO; PR:P25772; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IDA:EcoCyc.
DR GO; GO:0006288; P:base-excision repair, DNA ligation; IBA:GO_Central.
DR GO; GO:0006266; P:DNA ligation; IDA:EcoCyc.
DR GO; GO:0051103; P:DNA ligation involved in DNA repair; IMP:EcoCyc.
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 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese; NAD;
KW Reference proteome.
FT CHAIN 1..560
FT /note="DNA ligase B"
FT /id="PRO_0000161776"
FT ACT_SITE 124
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 124
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11812821"
SQ SEQUENCE 560 AA; 63179 MW; 2C1BA1F9B247A599 CRC64;
MKVWMAILIG ILCWQSSVWA VCPAWSPARA QEEISRLQQQ IKQWDDDYWK EGKSEVEDGV
YDQLSARLTQ WQRCFGSEPR DVMMPPLNGA VMHPVAHTGV RKMVDKNALS LWMRERSDLW
VQPKVDGVAV TLVYRDGKLN KAISRGNGLK GEDWTQKVSL ISAVPQTVSG PLANSTLQGE
IFLQREGHIQ QQMGGINARA KVAGLMMRQD DSDTLNSLGV FVWAWPDGPQ LMSDRLKELA
TAGFTLTQTY TRAVKNADEV ARVRNEWWKA ELPFVTDGVV VRAAKEPESR HWLPGQAEWL
VAWKYQPVAQ VAEVKAIQFA VGKSGKISVV ASLAPVMLDD KKVQRVNIGS VRRWQEWDIA
PGDQILVSLA GQGIPRIDDV VWRGAERTKP TPPENRFNSL TCYFASDVCQ EQFISRLVWL
GAKQVLGLDG IGEAGWRALH QTHRFEHIFS WLLLTPEQLQ NTPGIAKSKS AQLWHQFNLA
RKQPFTRWVM AMGIPLTRAA LNASDERSWS QLLFSTEQFW QQLPGTGSGR ARQVIEWKEN
AQIKKLGSWL AAQQITGFEP