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Protein data for DNLJ_ECOLI:

Description:
DNA ligase (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD+]).

Molecular weight: 73606

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
07-MAR-2006, entry version 67.

Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein DNLJ_ECOLI:

DatabasePointerAdd. info#1Add. info#2
EMBLM30255AAA24071.1-
EMBLM24278AAA24070.1-
EMBLU00096AAC75464.1-
EMBLD90870BAA16283.1ALT_FRAME
EMBLD90870BAA16282.1ALT_FRAME
EMBLU74650AAB42062.1-
PIRB65015LQECC6.
HSSPO877031B04
GenomeReviewsU00096_GRb2411.1
EchoBASEEB0529-.1
EcoGeneEG10534ligA.
BioCycEcoCyc:EG10534-MONOMER-.1
GOGO:0005515F:protein bindingIPI.
InterProIPR001357BRCT.
InterProIPR004150DNA_ligase_OB.
InterProIPR001679DNAligase.
InterProIPR000445HhH.
InterProIPR003583HHH1_bd.
InterProIPR004149Znf_DNAligase_C4.
PANTHERPTHR11107DNAligase.11.
PfamPF00533BRCT1.
PfamPF01653DNA_ligase_aden1.
PfamPF03120DNA_ligase_OB1.
PfamPF03119DNA_ligase_ZBD1.
PfamPF00633HHH1.
ProDomPD003944DNAligase1.
SMARTSM00292BRCT1.
SMARTSM00278HhH12.
SMARTSM00532LIGANc1.
TIGRFAMsTIGR00575dnlj1.
PROSITEPS50172BRCT1.
PROSITEPS01055DNA_LIGASE_N11.
PROSITEPS01056DNA_LIGASE_N21.

General information about the databases mentioned above

Keywords:
Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; Ligase; NAD.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-13 AND
RP 666-671.
RC STRAIN=K12 / C600;
RX MEDLINE=86310292; PubMed=3018436; DOI=10.1007/BF00330179;
RA Ishino Y., Shinagawa H., Makino K., Tsunasawa S., Sakiyama F.,
RA Nakata A.;
RT "Nucleotide sequence of the lig gene and primary structure of DNA
RT ligase of Escherichia coli.";
RL Mol. Gen. Genet. 204:1-7(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA O'Connor M.J., Ally A., Ally D., Zhang X., Robichaud M., Backman K.;
RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
RC STRAIN=PB103;
RX MEDLINE=97160838; PubMed=9008158; DOI=10.1016/S0092-8674(00)81838-3;
RA Hale C.A., de Boer P.A.J.;
RT "Direct binding of FtsZ to ZipA, an essential component of the septal
RT ring structure that mediates cell division in E. coli.";
RL Cell 88:175-185(1997).

Feature:
CHAIN 1 671 DNA ligase.
/FTId=PRO_0000161745.
DOMAIN 593 671 BRCT.
ACT_SITE 115 115 N6-AMP-lysine intermediate (By
similarity).
CONFLICT 69 69 A -> R (in Ref. 1).

Comments:
-!- FUNCTION: This protein catalyzes the formation of phosphodiester
linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
stranded DNA using NAD as a coenzyme and as the energy source for
the reaction. It is essential for DNA replication and repair of
damaged DNA.
-!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) +
(deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide +
(deoxyribonucleotide)(n+m).
-!- INTERACTION:
P06958:aceE; NbExp=1; IntAct=EBI-553496, EBI-542683;
P07813:leuS; NbExp=1; IntAct=EBI-553496, EBI-553345;
P21645:lpxD; NbExp=1; IntAct=EBI-553496, EBI-542924;
P16926:mreC; NbExp=1; IntAct=EBI-553496, EBI-553515;
P36767:rdgC; NbExp=1; IntAct=EBI-553496, EBI-561716;
P15032:recE; NbExp=1; IntAct=EBI-553496, EBI-553304;
P0A7K2:rplL; NbExp=1; IntAct=EBI-553496, EBI-543702;
P0A7V0:rpsB; NbExp=1; IntAct=EBI-553496, EBI-543439;
P77212:ykgC; NbExp=1; IntAct=EBI-553496, EBI-553523;
-!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family.
-!- SIMILARITY: Contains 1 BRCT domain.
-!- CAUTION: Ref.4 sequence differs from that shown due to frameshifts
in positions 289 and 313.
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Sequence length: 671

     MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP ELITPDSPTQ
     RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD RLKNNEKVTW CCELKLDGLA
     VSILYENGVL VSAATRGDGT TGEDITSNVR TIRAIPLKLH GENIPARLEV RGEVFLPQAG
     FEKINEDARR TGGKVFANPR NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL
     GRLLQFKKWG LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL
     GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG VLVSNATLHN
     ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR EVVFPTHCPV CGSDVERVEG
     EAVARCTGGL ICGAQRKESL KHFVSRRAMD VDGMGDKIID QLVEKEYVHT PADLFKLTAG
     KLTGLERMGP KSAQNVVNAL EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA
     ASIEELQKVP DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG
     KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA KAQELGIEVI
     DEAEMLRLLG S

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