YFJP_BACSU
ID YFJP_BACSU Reviewed; 287 AA.
AC O31544; Q79F09;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative DNA-3-methyladenine glycosylase YfjP;
DE EC=3.2.2.21;
GN Name=yfjP; OrderedLocusNames=BSU08010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT region of the Bacillus subtilis chromosome containing genes for trehalose
RT metabolism and acetoin utilization.";
RL Microbiology 142:3057-3065(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-
CC methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and
CC O2-methylcytosine from the damaged DNA polymer formed by alkylation
CC lesions. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC {ECO:0000305}.
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DR EMBL; D78509; BAA24301.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12630.1; -; Genomic_DNA.
DR PIR; G69806; G69806.
DR RefSeq; NP_388682.1; NC_000964.3.
DR RefSeq; WP_003233646.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31544; -.
DR SMR; O31544; -.
DR STRING; 224308.BSU08010; -.
DR PaxDb; O31544; -.
DR PRIDE; O31544; -.
DR EnsemblBacteria; CAB12630; CAB12630; BSU_08010.
DR GeneID; 939192; -.
DR KEGG; bsu:BSU08010; -.
DR PATRIC; fig|224308.179.peg.866; -.
DR eggNOG; COG0122; Bacteria.
DR InParanoid; O31544; -.
DR OMA; YLWRSIE; -.
DR PhylomeDB; O31544; -.
DR BioCyc; BSUB:BSU08010-MON; -.
DR PRO; PR:O31544; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0032131; F:alkylated DNA binding; IBA:GO_Central.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IBA:GO_Central.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IBA:GO_Central.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central.
DR CDD; cd00056; ENDO3c; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Hydrolase; Reference proteome.
FT CHAIN 1..287
FT /note="Putative DNA-3-methyladenine glycosylase YfjP"
FT /id="PRO_0000360864"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT SITE 222
FT /note="Determinant for substrate specificity and/or
FT activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 287 AA; 33178 MW; 89790D5090FDE589 CRC64;
MWKEKVSVTP PYHFDRVLDR LSLDPLNAVD REAREVRVPI RNQAGDVCIV KVQALGHAGE
PEFLVSGETD QGEMMKEIKR IFQWENHLQH VLDHFSKTSL SAIFEEHAGT PLVLDYSVYN
CMMKCIIHQQ LNLSFAYTLT ERFVHAFGEQ KDGVWCYPKP ETIAELDYQD LRDLQFSMRK
AEYTIDTSRM IAEGTLSLSE LPHMADEDIM KKLIKIRGIG PWTVQNVLMF GLGRPNLFPL
ADIGLQNAIK RHFQLDDKPA KDVMLAMSKE WEPYLSYASL YLWRSIE
