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DNA base-flipping protein (Alkyltransferase-like protein ATL)

 ATL_ECOLI               Reviewed;         129 AA.
P0AFP2; P75707; P77119; Q2MBX2;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
28-MAR-2018, entry version 99.
RecName: Full=DNA base-flipping protein {ECO:0000303|PubMed:18084297};
AltName: Full=Alkyltransferase-like protein ATL {ECO:0000303|PubMed:16027108};
Name=atl {ECO:0000303|PubMed:16027108};
Synonyms=ybaZ {ECO:0000303|PubMed:18084297};
OrderedLocusNames=b0454, JW0444;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
FUNCTION, DNA-BINDING, AND MUTAGENESIS OF TRP-83.
PubMed=16027108; DOI=10.1093/nar/gki696;
Pearson S.J., Ferguson J., Santibanez-Koref M., Margison G.P.;
"Inhibition of O6-methylguanine-DNA methyltransferase by an
alkyltransferase-like protein from Escherichia coli.";
Nucleic Acids Res. 33:3837-3844(2005).
[5]
FUNCTION, DNA-BINDING, AND INTERACTION WITH HELD.
STRAIN=K12;
PubMed=18084297; DOI=10.1038/nmeth1148;
Chen C.S., Korobkova E., Chen H., Zhu J., Jian X., Tao S.C., He C.,
Zhu H.;
"A proteome chip approach reveals new DNA damage recognition
activities in Escherichia coli.";
Nat. Methods 5:69-74(2008).
[6]
FUNCTION, DNA-BINDING, AND INTERACTION WITH UVRA.
STRAIN=K12 / AB1157;
PubMed=19269902; DOI=10.1016/j.dnarep.2009.01.022;
Mazon G., Philippin G., Cadet J., Gasparutto D., Fuchs R.P.;
"The alkyltransferase-like ybaZ gene product enhances nucleotide
excision repair of O(6)-alkylguanine adducts in E. coli.";
DNA Repair 8:697-703(2009).
[7]
FUNCTION.
PubMed=20921378; DOI=10.1073/pnas.1008635107;
Mazon G., Philippin G., Cadet J., Gasparutto D., Modesti M.,
Fuchs R.P.;
"Alkyltransferase-like protein (eATL) prevents mismatch repair-
mediated toxicity induced by O6-alkylguanine adducts in Escherichia
coli.";
Proc. Natl. Acad. Sci. U.S.A. 107:18050-18055(2010).
-!- FUNCTION: Involved in DNA damage recognition. Binds DNA containing
O(6)-methylguanine and larger O(6)-alkylguanine adducts, and to
double-stranded DNA that contains an AP (apurinic/apyrimidinic)
site (PubMed:16027108, PubMed:18084297, PubMed:19269902,
PubMed:20921378). Binds to the damaged base and flips the base out
of the DNA duplex into an extrahelical conformation, which allows
processing by repair proteins (PubMed:18084297). Works in
partnership with the nucleotide excision repair (NER) pathway to
enhance the repair of the O(6)-alkylguanine adducts larger than
the methyl adduct (PubMed:19269902, PubMed:20921378). Also
prevents methyl-directed mismatch repair (MMR)-mediated attack of
the O(6)-alkylguanine:T mispairs for the larger alkyl groups
(PubMed:20921378). {ECO:0000269|PubMed:16027108,
ECO:0000269|PubMed:18084297, ECO:0000269|PubMed:19269902,
ECO:0000269|PubMed:20921378}.
-!- SUBUNIT: Interacts with HelD and UvrA.
{ECO:0000269|PubMed:18084297, ECO:0000269|PubMed:19269902}.
-!- INTERACTION:
P0A698:uvrA; NbExp=2; IntAct=EBI-560039, EBI-552091;
-!- MISCELLANEOUS: Does not have alkyltransferase activity. A
tryptophan residue replaces the cysteine at the known active site
of MGMT. {ECO:0000269|PubMed:16027108}.
-!- SIMILARITY: Belongs to the MGMT family. ATL subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB40210.1; Type=Frameshift; Positions=64; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U82664; AAB40210.1; ALT_FRAME; Genomic_DNA.
EMBL; U00096; AAC73557.1; -; Genomic_DNA.
EMBL; AP009048; BAE76234.1; -; Genomic_DNA.
PIR; F64775; F64775.
RefSeq; NP_414988.1; NC_000913.3.
RefSeq; WP_001300427.1; NZ_LN832404.1.
ProteinModelPortal; P0AFP2; -.
SMR; P0AFP2; -.
BioGrid; 4259845; 66.
DIP; DIP-48135N; -.
IntAct; P0AFP2; 16.
STRING; 316385.ECDH10B_0410; -.
PaxDb; P0AFP2; -.
PRIDE; P0AFP2; -.
EnsemblBacteria; AAC73557; AAC73557; b0454.
EnsemblBacteria; BAE76234; BAE76234; BAE76234.
GeneID; 945094; -.
KEGG; ecj:JW0444; -.
KEGG; eco:b0454; -.
PATRIC; fig|511145.12.peg.473; -.
EchoBASE; EB3043; -.
EcoGene; EG13254; ybaZ.
eggNOG; ENOG41080UX; Bacteria.
eggNOG; COG3695; LUCA.
HOGENOM; HOG000244138; -.
InParanoid; P0AFP2; -.
KO; K07443; -.
OMA; WHRVINA; -.
PhylomeDB; P0AFP2; -.
BioCyc; EcoCyc:G6251-MONOMER; -.
PRO; PR:P0AFP2; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0003824; F:catalytic activity; IEA:InterPro.
GO; GO:0003684; F:damaged DNA binding; IDA:EcoCyc.
GO; GO:0019899; F:enzyme binding; IPI:EcoCyc.
GO; GO:0006281; P:DNA repair; IEA:InterPro.
CDD; cd06445; ATase; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF01035; DNA_binding_1; 1.
SUPFAM; SSF46767; SSF46767; 1.
TIGRFAMs; TIGR00589; ogt; 1.
1: Evidence at protein level;
Complete proteome; DNA damage; DNA-binding; Reference proteome.
CHAIN 1 129 DNA base-flipping protein.
/FTId=PRO_0000139390.
SITE 52 52 Required for phosphate
rotation/nucleotide flipping.
{ECO:0000250|UniProtKB:Q9UTN9}.
SITE 66 66 Arg finger, required for nucleotide
flipping. {ECO:0000250|UniProtKB:Q9UTN9}.
MUTAGEN 83 83 W->C: Does not confer alkyltransferase
activity. {ECO:0000269|PubMed:16027108}.
SEQUENCE 129 AA; 14450 MW; 584382A5657919CA CRC64;
MLVSCAMRLH SGVFPDYAEK LPQEEKMEKE DSFPQRVWQI VAAIPEGYVT TYGDVAKLAG
SPRAARQVGG VLKRLPEGST LPWHRVVNRH GTISLTGPDL QRQRQALLAE GVMVSGSGQI
DLQRYRWNY


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