DNLI_HAEIN
ID DNLI_HAEIN Reviewed; 268 AA.
AC P44121; P44122; P71371; P71372;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.1;
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN Name=ligA; OrderedLocusNames=HI_1182/HI_1183;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=8550458; DOI=10.1128/jb.178.2.396-402.1996;
RA Preston A., Maskell D., Johnson A., Moxon E.R.;
RT "Altered lipopolysaccharide characteristic of the I69 phenotype in
RT Haemophilus influenzae results from mutations in a novel gene, isn.";
RL J. Bacteriol. 178:396-402(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9060431; DOI=10.1093/nar/25.7.1369;
RA Cheng C., Shuman S.;
RT "Characterization of an ATP-dependent DNA ligase encoded by Haemophilus
RT influenzae.";
RL Nucleic Acids Res. 25:1369-1374(1997).
CC -!- FUNCTION: Catalyzes efficient strand joining on a single nicked DNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally proposed to code for two separate adjacent
CC ORFs, HI_1182 and HI_1183. {ECO:0000305|PubMed:7542800}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22836.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC22846.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U17295; AAA95982.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22836.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L42023; AAC22846.1; ALT_FRAME; Genomic_DNA.
DR PIR; D64021; D64021.
DR PIR; E64021; E64021.
DR AlphaFoldDB; P44121; -.
DR SMR; P44121; -.
DR STRING; 71421.HI_1182; -.
DR EnsemblBacteria; AAC22836; AAC22836; HI_1182.
DR EnsemblBacteria; AAC22846; AAC22846; HI_1183.
DR KEGG; hin:HI_1182; -.
DR KEGG; hin:HI_1183; -.
DR eggNOG; COG1793; Bacteria.
DR HOGENOM; CLU_1459372_0_0_6; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
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 InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR029319; DNA_ligase_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication;
KW Ligase; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..268
FT /note="DNA ligase"
FT /id="PRO_0000059625"
FT ACT_SITE 41
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 93
FT /note="T -> S (in Ref. 2; AAC22836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 30896 MW; F9EF9DD95B6B1252 CRC64;
MKFYRTLLLF FASSFAFANS DLMLLHTYNN QPIEGWVMSE KLDGVRGYWN GKQLLTRQGQ
RLSPPAYFIK DFPPFAIDGE LFSERNHFEE ISTITKSFKG DGWEKLKLYV FDVPDAEGNL
FERLAKLKAH LLEHPTTYIE IIEQIPVKDK THLYQFLAQV ENLQGEGVVV RNPNAPYERK
RSSQILKLKT ARGEECTVIA HHKGKGQFEN VMGALTCKNH RGEFKIGSGF NLNERENPPP
IGSVITYKYR GITNSGKPRF ATYWREKK
