ID   ATL_ECOLI               Reviewed;         129 AA.
AC   P0AFP2; P75707; P77119; Q2MBX2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=DNA base-flipping protein {ECO:0000303|PubMed:18084297};
DE   AltName: Full=Alkyltransferase-like protein ATL {ECO:0000303|PubMed:16027108};
GN   Name=atl {ECO:0000303|PubMed:16027108};
GN   Synonyms=ybaZ {ECO:0000303|PubMed:18084297};
GN   OrderedLocusNames=b0454, JW0444;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, DNA-BINDING, AND MUTAGENESIS OF TRP-83.
RX   PubMed=16027108; DOI=10.1093/nar/gki696;
RA   Pearson S.J., Ferguson J., Santibanez-Koref M., Margison G.P.;
RT   "Inhibition of O6-methylguanine-DNA methyltransferase by an
RT   alkyltransferase-like protein from Escherichia coli.";
RL   Nucleic Acids Res. 33:3837-3844(2005).
RN   [5]
RP   FUNCTION, DNA-BINDING, AND INTERACTION WITH HELD.
RC   STRAIN=K12;
RX   PubMed=18084297; DOI=10.1038/nmeth1148;
RA   Chen C.S., Korobkova E., Chen H., Zhu J., Jian X., Tao S.C., He C., Zhu H.;
RT   "A proteome chip approach reveals new DNA damage recognition activities in
RT   Escherichia coli.";
RL   Nat. Methods 5:69-74(2008).
RN   [6]
RP   FUNCTION, DNA-BINDING, AND INTERACTION WITH UVRA.
RC   STRAIN=K12 / AB1157;
RX   PubMed=19269902; DOI=10.1016/j.dnarep.2009.01.022;
RA   Mazon G., Philippin G., Cadet J., Gasparutto D., Fuchs R.P.;
RT   "The alkyltransferase-like ybaZ gene product enhances nucleotide excision
RT   repair of O(6)-alkylguanine adducts in E. coli.";
RL   DNA Repair 8:697-703(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=20921378; DOI=10.1073/pnas.1008635107;
RA   Mazon G., Philippin G., Cadet J., Gasparutto D., Modesti M., Fuchs R.P.;
RT   "Alkyltransferase-like protein (eATL) prevents mismatch repair-mediated
RT   toxicity induced by O6-alkylguanine adducts in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:18050-18055(2010).
CC   -!- FUNCTION: Involved in DNA damage recognition. Binds DNA containing
CC       O(6)-methylguanine and larger O(6)-alkylguanine adducts, and to double-
CC       stranded DNA that contains an AP (apurinic/apyrimidinic) site
CC       (PubMed:16027108, PubMed:18084297, PubMed:19269902, PubMed:20921378).
CC       Binds to the damaged base and flips the base out of the DNA duplex into
CC       an extrahelical conformation, which allows processing by repair
CC       proteins (PubMed:18084297). Works in partnership with the nucleotide
CC       excision repair (NER) pathway to enhance the repair of the O(6)-
CC       alkylguanine adducts larger than the methyl adduct (PubMed:19269902,
CC       PubMed:20921378). Also prevents methyl-directed mismatch repair (MMR)-
CC       mediated attack of the O(6)-alkylguanine:T mispairs for the larger
CC       alkyl groups (PubMed:20921378). {ECO:0000269|PubMed:16027108,
CC       ECO:0000269|PubMed:18084297, ECO:0000269|PubMed:19269902,
CC       ECO:0000269|PubMed:20921378}.
CC   -!- SUBUNIT: Interacts with HelD and UvrA. {ECO:0000269|PubMed:18084297,
CC       ECO:0000269|PubMed:19269902}.
CC   -!- INTERACTION:
CC       P0AFP2; P0A698: uvrA; NbExp=2; IntAct=EBI-560039, EBI-552091;
CC   -!- MISCELLANEOUS: Does not have alkyltransferase activity. A tryptophan
CC       residue replaces the cysteine at the known active site of MGMT.
CC       {ECO:0000269|PubMed:16027108}.
CC   -!- SIMILARITY: Belongs to the MGMT family. ATL subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40210.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U82664; AAB40210.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAC73557.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76234.1; -; Genomic_DNA.
DR   PIR; F64775; F64775.
DR   RefSeq; NP_414988.1; NC_000913.3.
DR   RefSeq; WP_001300427.1; NZ_SSZK01000009.1.
DR   AlphaFoldDB; P0AFP2; -.
DR   SMR; P0AFP2; -.
DR   BioGRID; 4259845; 66.
DR   DIP; DIP-48135N; -.
DR   IntAct; P0AFP2; 16.
DR   STRING; 511145.b0454; -.
DR   PaxDb; P0AFP2; -.
DR   PRIDE; P0AFP2; -.
DR   EnsemblBacteria; AAC73557; AAC73557; b0454.
DR   EnsemblBacteria; BAE76234; BAE76234; BAE76234.
DR   GeneID; 945094; -.
DR   KEGG; ecj:JW0444; -.
DR   KEGG; eco:b0454; -.
DR   PATRIC; fig|511145.12.peg.473; -.
DR   EchoBASE; EB3043; -.
DR   eggNOG; COG3695; Bacteria.
DR   HOGENOM; CLU_000445_52_5_6; -.
DR   InParanoid; P0AFP2; -.
DR   OMA; PRHSRHV; -.
DR   PhylomeDB; P0AFP2; -.
DR   BioCyc; EcoCyc:G6251-MON; -.
DR   PRO; PR:P0AFP2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:EcoCyc.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd06445; ATase; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR   InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   SUPFAM; SSF46767; SSF46767; 1.
DR   TIGRFAMs; TIGR00589; ogt; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA-binding; Reference proteome.
FT   CHAIN           1..129
FT                   /note="DNA base-flipping protein"
FT                   /id="PRO_0000139390"
FT   SITE            52
FT                   /note="Required for phosphate rotation/nucleotide flipping"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UTN9"
FT   SITE            66
FT                   /note="Arg finger, required for nucleotide flipping"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UTN9"
FT   MUTAGEN         83
FT                   /note="W->C: Does not confer alkyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:16027108"
SQ   SEQUENCE   129 AA;  14450 MW;  584382A5657919CA CRC64;
     MLVSCAMRLH SGVFPDYAEK LPQEEKMEKE DSFPQRVWQI VAAIPEGYVT TYGDVAKLAG
     SPRAARQVGG VLKRLPEGST LPWHRVVNRH GTISLTGPDL QRQRQALLAE GVMVSGSGQI
     DLQRYRWNY