LIGB_YERPS
ID LIGB_YERPS Reviewed; 567 AA.
AC Q66GE4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=YPTB0038;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19278.1; -; Genomic_DNA.
DR RefSeq; WP_011191447.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66GE4; -.
DR SMR; Q66GE4; -.
DR EnsemblBacteria; CAH19278; CAH19278; YPTB0038.
DR GeneID; 66843566; -.
DR KEGG; ypo:BZ17_2557; -.
DR KEGG; yps:YPTB0038; -.
DR PATRIC; fig|273123.14.peg.2682; -.
DR OMA; DLWIQPK; -.
DR Proteomes; UP000001011; 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 CDD; cd00114; LIGANc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01587; DNA_ligase_B; 1.
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 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.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; NAD.
FT CHAIN 1..567
FT /note="DNA ligase B"
FT /id="PRO_0000313562"
FT ACT_SITE 132
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01587"
SQ SEQUENCE 567 AA; 63623 MW; EFE6A7D5BCE2951F CRC64;
MNILNLKIIM FLLISNIIVV GGAWATSTCP DWPATRIAVE INALEQQLNK WSAAYHQQGH
SPVTDDIYDQ LQDKLRVWQS CRGLPDKTES QPIPGKGQFL HPVAHTGLKK LKDETALTRW
MAGRKNLWVQ PKVDGVAVTL VYHGGKLVQL LSRGNGVKGQ NWTEKAPFIS AIPQYIANAP
ALLTLQGELF LLMDGHQQAK SGGVNARSTV AGALMRKSPS PLLAQVGVFI WAWPDGPTTM
KEKVALLQVM GFPFTAKYSE PVMSHLDVVQ WRQFWFQAPL PFVTDGVVVR QEEEPAGRYW
QATPGQWSMA WKYPPLQHIA EVKDIHFTLG RTGKGTVVLE VLPIKIDDKW IRRVNIGSVT
RWKQWDIAPG DHITLALAGH GIPRLDNVVW RVHQRNTITA PNWDKFHQLS CFQRLPHGCE
PQFLSRLIWL SGPGGLDIGG IGGGFWQKLI HHELINDLVG WLLLTPEQIA SIPGIGNARA
EKIYQQFQRA KQQPFSRWLL ALGFPQVVSV DAQWQVVLRR SLSEWATMAG IGQMRAKQIK
HFLDHPDVQA LADFLSTQKV VGFELTE