PGLX_LACCZ
ID PGLX_LACCZ Reviewed; 1202 AA.
AC P0DQP1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Adenine-specific methyltransferase PglX {ECO:0000303|PubMed:31399407};
DE EC=2.1.1.72 {ECO:0000305|PubMed:31399407};
DE AltName: Full=BREX protein PglX {ECO:0000305};
GN Name=pglX {ECO:0000303|PubMed:31399407}; OrderedLocusNames=LCAZH_2056;
OS Lacticaseibacillus casei (strain Zhang) (Lactobacillus casei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=498216;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhang;
RX PubMed=20675486; DOI=10.1128/jb.00802-10;
RA Zhang W., Yu D., Sun Z., Wu R., Chen X., Chen W., Meng H., Hu S., Zhang H.;
RT "Complete genome sequence of Lactobacillus casei Zhang, a new probiotic
RT strain isolated from traditional homemade koumiss in Inner Mongolia,
RT China.";
RL J. Bacteriol. 192:5268-5269(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], DISCUSSION OF FUNCTION, AND
RP DNA METHYLOME.
RC STRAIN=Zhang;
RX PubMed=25747834; DOI=10.3168/jds.2014-9272;
RA Zhang W., Sun Z., Menghe B., Zhang H.;
RT "Short communication: Single molecule, real-time sequencing technology
RT revealed species- and strain-specific methylation patterns of 2
RT Lactobacillus strains.";
RL J. Dairy Sci. 98:3020-3024(2015).
RN [3]
RP CLASSIFICATION AND NOMENCLATURE.
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).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Zhang;
RX PubMed=31399407; DOI=10.1128/aem.01001-19;
RA Hui W., Zhang W., Kwok L.Y., Zhang H., Kong J., Sun T.;
RT "A Novel Bacteriophage Exclusion (BREX) System Encoded by the pglX Gene in
RT Lactobacillus casei Zhang.";
RL Appl. Environ. Microbiol. 85:0-0(2019).
CC -!- FUNCTION: BREX systems (bacteriophage exclusion) provide immunity
CC against bacteriophage. Part of a type 1 BREX system which protects
CC against dsDNA phage (Probable). This system allows phage adsorption but
CC prevents phage DNA replication, without degradation of the phage DNA.
CC Methylation of bacterial DNA by this protein guides self/non-self
CC discrimination (By similarity). {ECO:0000250|UniProtKB:P0DUF9,
CC ECO:0000305|PubMed:25452498}.
CC -!- FUNCTION: Probably methylates the adenine in the fifth position of the
CC hexamer 5'-ACRCAG-3' in genomic DNA (Probable). N(6)-methylated adenine
CC on the fifth position of 5'-ACRCAG-3' is found in the genome; there are
CC 1906 sites in the genomic DNA (PubMed:25747834).
CC {ECO:0000269|PubMed:25747834, ECO:0000305|PubMed:31399407}.
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:25747834, ECO:0000305|PubMed:31399407};
CC -!- DISRUPTION PHENOTYPE: Loss of whole genome N(6)-adenine methylation in
CC the fifth position of the hexamer 5'-ACRCAG-3', no visible growth
CC phenotype. Has a higher plasmid acquisition ability (when plasmids have
CC the methylation hexamer) but a reduced ability to retain plasmids.
CC {ECO:0000269|PubMed:31399407}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PglX adenine
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; CP001084; ADK19266.1; -; Genomic_DNA.
DR RefSeq; WP_013245950.1; NC_014334.2.
DR AlphaFoldDB; P0DQP1; -.
DR GeneID; 61270228; -.
DR KEGG; lcz:LCAZH_2056; -.
DR OMA; RIIAIRF; -.
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; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Antiviral defense; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1202
FT /note="Adenine-specific methyltransferase PglX"
FT /id="PRO_0000452164"
SQ SEQUENCE 1202 AA; 138959 MW; 9A20B6F2B42801B0 CRC64;
MDKKAIKTFA IQARRSLIES IKLKLENLGI TKDGVAEKMS QSTNEIEYYG DKGLSITGQD
IRRRRELVAR LKGMAKQEEW SDALTDLIEE VAYTWFNRII AIRFMEVNEY LPSGVRVLSS
ETKLKVPDIL REAFEIEDDL GGYSVDEHGI IQKALDTEDP TDMDAAYVIL FTKQANALNH
YLPELFEKTD DFMQLLFTPS YSSGVIKDLV DDIKEDDFDV DEGGQVEIIG WLYQYYNTEP
KDAAFKKKKY LSSDIPAVTQ LFTPDWIVKY LVENSLGRYW IRVLHDRGDE RTSLQIAQSF
NWQYFMPEAK QDEISTRADL SKKRVEEITF VDPAMGSGHI LIYAFDVLLQ LYQSEGYSRR
EAAQNIVERN LFGLDIDRRA FQLTYFAMMM KLRRENRRSF ELQLHPNVFE VPSTSLELKD
FSGAKDGSPI DSGNLSDVLG RFGAGKELGS LITFESSIFD DKLINKIVSE REAGQLTFEM
SDQVNHQWEL RNLIRVGKAL SSQYTISVTN PPYMGSGKMP KTLAKFVGKY YPASKSDLFA
VFMERLQHLT KENGIFAMIT QHQWMFLSSF KALRERMSSW PIINMAHLGT RAFEEIGGEV
VQTTAFVVQK QKLQGFIGTY ERLVDFDSQK KKQQAFLTAV QNPNLNYVYR TKQTNFEKIP
GSPIAYWASK KKLELLQYSS YRLQNILSAR EGMTTGNNAL FMRSWHEVQF FKISFLSTAH
QIERDKTWFP YNKGGAFRKW YGNIWYVINW KNHGEAIQSN IDKKTGRIRS HNYNGKFGFR
EAITWSAISS GMFSARYSPT GFLFDSKGVS SFANDHTTLL FCLAFLNSNS SSSFLELLSP
TMDFKIGQVL NLPLAKQHSP QVVELTESLI SSSREDWNSF ENSWSFTTNI LLTNIAEHHR
NWTVEAAFQQ WQKEADDRFN QLKANEEELN RIFIDLYGLQ DELSPEEEDK DVSVRRANLP
RDIKAFISYF IGCVFGRYSI DTPGLAYAGG DWDASKYKTF IPNKDDLILL TDDDYFGDDR
DVMTRFKEFL TTTFGSENLN ENLKFIADAL GKRGDSSEEQ IRAYLRDDFF KKDHLSTYQK
RPIYWEFNSG RNGGFKALMY LHRYDRNTVA MIRTKYLHPL QEAYERKLVQ LKKFEENEQQ
TRQKNKYKKQ ITTITKELDE LIKYDEKLQH VANLHIDLDL DDGVLVNHAK AQADTKILTP
LK
