ID   ATL_THET8               Reviewed;         147 AA.
AC   Q5SI16;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=DNA base-flipping protein {ECO:0000250|UniProtKB:P0AFP2};
DE   AltName: Full=Alkyltransferase-like protein ATL {ECO:0000250|UniProtKB:P0AFP2};
GN   OrderedLocusNames=TTHA1564 {ECO:0000312|EMBL:BAD71387.1};
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RX   PubMed=18483064; DOI=10.1093/jb/mvn065;
RA   Morita R., Nakagawa N., Kuramitsu S., Masui R.;
RT   "An O6-methylguanine-DNA methyltransferase-like protein from Thermus
RT   thermophilus interacts with a nucleotide excision repair protein.";
RL   J. Biochem. 144:267-277(2008).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH RNA POLYMERASE.
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RX   PubMed=21531768; DOI=10.1093/jb/mvr052;
RA   Morita R., Hishinuma H., Ohyama H., Mega R., Ohta T., Nakagawa N.,
RA   Agari Y., Fukui K., Shinkai A., Kuramitsu S., Masui R.;
RT   "An alkyltransferase-like protein from Thermus thermophilus HB8 affects the
RT   regulation of gene expression in alkylation response.";
RL   J. Biochem. 150:327-339(2011).
RN   [4]
RP   FUNCTION.
RX   PubMed=23112169; DOI=10.1073/pnas.1209451109;
RA   Wilkinson O.J., Latypov V., Tubbs J.L., Millington C.L., Morita R.,
RA   Blackburn H., Marriott A., McGown G., Thorncroft M., Watson A.J.,
RA   Connolly B.A., Grasby J.A., Masui R., Hunter C.A., Tainer J.A.,
RA   Margison G.P., Williams D.M.;
RT   "Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for
RT   DNA repair using cation-pi interactions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:18755-18760(2012).
CC   -!- FUNCTION: Involved in DNA damage recognition. Binds DNA containing
CC       O(6)-methylguanine and larger O(6)-alkylguanine adducts
CC       (PubMed:18483064, PubMed:23112169). Binds to the damaged base and flips
CC       the base out of the DNA duplex into an extrahelical conformation, which
CC       allows processing by repair proteins (PubMed:18483064). Also affects
CC       the regulation of gene expression in response to alkylation
CC       (PubMed:21531768). {ECO:0000269|PubMed:18483064,
CC       ECO:0000269|PubMed:21531768}.
CC   -!- SUBUNIT: Interacts with several proteins, including UvrA, UvrD and the
CC       three subunits of the RNA polymerase. {ECO:0000269|PubMed:18483064,
CC       ECO:0000269|PubMed:21531768}.
CC   -!- DISRUPTION PHENOTYPE: Disruption increases the spontaneous mutation
CC       rate. {ECO:0000269|PubMed:18483064}.
CC   -!- SIMILARITY: Belongs to the MGMT family. ATL subfamily. {ECO:0000305}.
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DR   EMBL; AP008226; BAD71387.1; -; Genomic_DNA.
DR   RefSeq; WP_011228767.1; NC_006461.1.
DR   RefSeq; YP_144830.1; NC_006461.1.
DR   AlphaFoldDB; Q5SI16; -.
DR   SMR; Q5SI16; -.
DR   STRING; 300852.55772946; -.
DR   EnsemblBacteria; BAD71387; BAD71387; BAD71387.
DR   GeneID; 3168219; -.
DR   KEGG; ttj:TTHA1564; -.
DR   PATRIC; fig|300852.9.peg.1535; -.
DR   eggNOG; COG0350; Bacteria.
DR   HOGENOM; CLU_000445_52_2_0; -.
DR   OMA; INNPKSC; -.
DR   PhylomeDB; Q5SI16; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:InterPro.
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; IPR036631; MGMT_N_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   SUPFAM; SSF46767; SSF46767; 1.
DR   SUPFAM; SSF53155; SSF53155; 1.
DR   TIGRFAMs; TIGR00589; ogt; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA-binding; Reference proteome.
FT   CHAIN           1..147
FT                   /note="DNA base-flipping protein"
FT                   /id="PRO_0000432551"
FT   SITE            88
FT                   /note="Required for phosphate rotation/nucleotide flipping"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UTN9"
FT   SITE            100
FT                   /note="Arg finger, required for nucleotide flipping"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UTN9"
SQ   SEQUENCE   147 AA;  16258 MW;  918B339396E33E82 CRC64;
     MWLPTPLGPL WLEVSPLGVR RLEPALYPRG PEAEGALALR VREAVQAYFA GERPDFLDLP
     LDYTGLSPAR LRLYERVRLV PYGRTVSYGA LGRELGLSPR AVGAALRACP FFLLVPAHRV
     IHADGRLGGF QGQEGLKLWL LRFEGAL