ID   PGLX_BACCH              Reviewed;        1179 AA.
AC   P0DUF3;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Adenine-specific methyltransferase PglX {ECO:0000303|PubMed:25452498};
DE            EC=2.1.1.72 {ECO:0000305|PubMed:25452498};
DE   AltName: Full=BREX protein PglX {ECO:0000305};
GN   Name=pglX {ECO:0000303|PubMed:25452498}; ORFNames=BCH308197_0966;
OS   Bacillus cereus (strain H3081.97).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=451708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3081.97;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus H3081.97.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN ANTIVIRAL DEFENSE, FUNCTION AS A DNA METHYLASE, INDUCTION,
RP   DISRUPTION PHENOTYPE, AND CLASSIFICATION AND NOMENCLATURE.
RC   STRAIN=H3081.97;
RX   PubMed=25452498; DOI=10.15252/embj.201489455;
RA   Goldfarb T., Sberro H., Weinstock E., Cohen O., Doron S.,
RA   Charpak-Amikam Y., Afik S., Ofir G., Sorek R.;
RT   "BREX is a novel phage resistance system widespread in microbial genomes.";
RL   EMBO J. 34:169-183(2015).
CC   -!- FUNCTION: BREX systems (bacteriophage exclusion) provide immunity
CC       against bacteriophage. Part of a type 1 BREX system. This system allows
CC       phage adsorption but prevents phage DNA replication, without
CC       degradation of the phage DNA. Methylation of bacterial DNA by this
CC       protein probably guides self/non-self discrimination. When the brxA-
CC       brxB-brxC-pglX and pglZ-brxL operons are transformed into a susceptible
CC       B.subtilis strain (BEST7003) they confer resistance to bacteriophages
CC       SPbeta, SP16, Zeta, phi3T and SP02 and partial protection to phages
CC       SP01 and SP82G (these include lytic and temperate phage). They do not
CC       protect against phages phi105, rho10 or rho14. Additionally confers a
CC       very slight reduction in efficiency of plasmid transformation.
CC       {ECO:0000269|PubMed:25452498}.
CC   -!- FUNCTION: Methylates the adenine in the fifth position of the hexamer
CC       5'-TAGGAG-3' in genomic DNA but not in phage DNA upon infection.
CC       {ECO:0000269|PubMed:25452498}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000305|PubMed:25452498};
CC   -!- INDUCTION: Part of the brxA-brxB-brxC-pglX operon.
CC       {ECO:0000269|PubMed:25452498}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype during normal growth, BREX
CC       no longer confers phage resistance. {ECO:0000269|PubMed:25452498}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. PglX adenine
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; ABDL02000007; EDZ57596.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DUF3; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..1179
FT                   /note="Adenine-specific methyltransferase PglX"
FT                   /id="PRO_0000452162"
SQ   SEQUENCE   1179 AA;  138130 MW;  F3A7E3DE74087054 CRC64;
     MNKTAIKNFA VSARMKLIDA VKQKAYELGI TETEIKEPET YEDGFRINNK FFRSYELEQR
     KKLIQKIEEK DYKQVIEEVS YTWFNRFIAI RFMEVNEYLP TGVRVLSSTQ EGKNEPDVIG
     EVTNIAEDLD LNLDIVYRLQ DENKTEDLFK YILIKQCNKL GEIMPMMFET IQDYTELLLP
     DNLLGEGSVV RNLVSMIDEE DWKEQVEIIG WLYQYYISEK KDEVFADLKK NKKITKENIP
     AATQLFTPKW IVKYMVENSL GRLWLESHPN EDVQQQWKYY LEEAEQEPNV QEQLEKLKNN
     ELSPEDITVL DPCMGSGHIL VYAFDVLYNI YQHAGYSERE IPQLILEKNL YGLDIDDRAA
     QLAYFALMMK ARSYNRRIFR RPLELNVCSI QESNGIPQEA IDYFVGDSLD RDEITYLIRV
     FEDSKEYGSI LEVLSIDFVS IEKRMIEIQE MQEVKDIFSL QYSDILLIKI PQLIKQAKIM
     SSKYHVVLTN PPYMGSKGMN EQLKKYCTKF FKKGKRDLFA VLMLKCFNFT KEGGYISNIN
     QQSWMFLSSY EEIRKYFLSE STICSMIHLG SGSFEEINGE VVQSTSFVLK KQVVKNYQTP
     FIRLVEYNDS QEKKLSFLEK KERYIVAADL FLNVPGYQIA YWATQKMLVA FSENKVLGDL
     YDPRQGLATG DNDRFLRLWH EVDKVRINWG ALSISDAHES KIKWFPHNKG GRFRKWYGNN
     EYLISFNIES YNTLAKQGNC LPSKQLYFKS GITWSRTTSN LLGVRLHNQG TIFDCEGCFL
     SAGNTRDDYY LMAFLNSNVA FVFLEKINPT LHFQVGDVRK IPLMTFNNLL EAKMDLITSC
     ISISKRDWDS FETSWGFIRH PMLTHKNSSR RLSEVLDYWS VFAEQQFNQL KANEEELNRI
     FIEIYDLQDD LTPEVKEKDI VIRKADKERD IKSFISYAVG CMLGRYSLDQ EGLVFAGGEF
     DESKYKTFKA DTDNIIPITD DEYFEDDIVS RFIEFVRVTF SEETLEENLD FIAEALNKKA
     NETSRQCIRR YFLKDFFKDH VKMYQKRPIY WLFDSGKNDG FKALVYMHRY DVGTVAEVRT
     DYLHTLQRKY EAEIARRDVL LESDASTKDK TRAKKEKEKL QKQLLECQQY DQVIAHIANQ
     KITIDLDDGV KVNYAKFQNV ELPQGEGKKP LKANLLAKI