ID Q4QLB6_HAEI8 Unreviewed; 304 AA.
AC Q4QLB6;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=DNA ligase {ECO:0000313|EMBL:AAX88181.1};
DE EC=6.5.1.1 {ECO:0000313|EMBL:AAX88181.1};
GN Name=ligA {ECO:0000313|EMBL:AAX88181.1};
GN OrderedLocusNames=NTHI1352 {ECO:0000313|EMBL:AAX88181.1};
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310 {ECO:0000313|EMBL:AAX88181.1, ECO:0000313|Proteomes:UP000002525};
RN [1] {ECO:0000313|EMBL:AAX88181.1, ECO:0000313|Proteomes:UP000002525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP {ECO:0000313|EMBL:AAX88181.1,
RC ECO:0000313|Proteomes:UP000002525};
RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S.Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; Evidence={ECO:0000256|ARBA:ARBA00034003};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR EMBL; CP000057; AAX88181.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4QLB6; -.
DR KEGG; hit:NTHI1352; -.
DR HOGENOM; CLU_021047_0_0_6; -.
DR Proteomes; UP000002525; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000313|EMBL:AAX88181.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..258
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 304 AA; 35351 MW; 8B39A33001B7C539 CRC64;
MIFCDLDRKN KFEWLDIFQD MFILRKLISP LIFKNTMKFY RTLLLFFASS FAFANSDLML
LHTYNNQPIE GWVMSEKLDG VRGYWNGKQL LTRQGQPLSP PAYFIKDFPP FAIDGELFSE
RNHFEEISSI TKSFKGDGWA KLKLYVFDVP DAEGNLFERL AKLKAYLLEY PTTYIEIIEQ
IPVKDKTHLY QFLAQVENLQ GEGVVVRNPN APYERKRSSQ ILKLKTARDE ECTVIAHHKG
KGQFENVMGA LTCKNHRGEF KIGSGFNLNE RENPPPIGSV ITYKYRGITN SGKPRFATYW
REKK
//
