PGLX_STRCO
ID PGLX_STRCO Reviewed; 1210 AA.
AC Q8CJM2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Adenine-specific methyltransferase PglX {ECO:0000303|PubMed:25592393};
DE EC=2.1.1.72 {ECO:0000269|PubMed:25592393};
DE AltName: Full=Bacteriophage (PhiC31) resistance gene PglX {ECO:0000303|PubMed:11972785};
DE AltName: Full=Putative type II restriction enzyme and methyltransferase RM.ScoA3ORF6627P {ECO:0000303|PubMed:12654995};
DE Short=RM.ScoA3ORF6627P {ECO:0000303|PubMed:12654995};
GN Name=pglX {ECO:0000303|PubMed:11972785}; Synonyms=SC1F2.24;
GN OrderedLocusNames=SCO6627;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP GENETIC ANALYSIS, AND PHASE REVERSION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=8446035; DOI=10.1111/j.1365-2958.1993.tb01124.x;
RA Laity C., Chater K.F., Lewis C.G., Buttner M.J.;
RT "Genetic analysis of the phi C31-specific phage growth limitation (Pgl)
RT system of Streptomyces coelicolor A3(2).";
RL Mol. Microbiol. 7:329-336(1993).
RN [3]
RP FUNCTION IN ANTIVIRAL DEFENSE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=11972785; DOI=10.1046/j.1365-2958.2002.02896.x;
RA Sumby P., Smith M.C.;
RT "Genetics of the phage growth limitation (Pgl) system of Streptomyces
RT coelicolor A3(2).";
RL Mol. Microbiol. 44:489-500(2002).
RN [4]
RP INVOLVED IN PHASE VARIATION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12867465; DOI=10.1128/jb.185.15.4558-4563.2003;
RA Sumby P., Smith M.C.;
RT "Phase variation in the phage growth limitation system of Streptomyces
RT coelicolor A3(2).";
RL J. Bacteriol. 185:4558-4563(2003).
RN [5]
RP NOMENCLATURE, AND SUBTYPE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
RN [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-381.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=25592393; DOI=10.1016/j.virol.2014.12.036;
RA Hoskisson P.A., Sumby P., Smith M.C.M.;
RT "The phage growth limitation system in Streptomyces coelicolor A(3)2 is a
RT toxin/antitoxin system, comprising enzymes with DNA methyltransferase,
RT protein kinase and ATPase activity.";
RL Virology 477:100-109(2015).
CC -!- FUNCTION: BREX systems (bacteriophage exclusion) provide immunity
CC against bacteriophage. Part of a type 2 BREX system (Probable).
CC Probably a DNA methyltransferase, it methylates phage DNA in vitro in
CC an S-adenosyl-L-methionine-dependent manner (PubMed:25592393).
CC Previously called the phage growth limitation (Pgl) system, it confers
CC protection against bacteriophage phiC31. The bacteria allows one cycle
CC of phage infection, but subsequent cycles are impaired, protecting the
CC original bacterial colony (Probable). The system undergoes high rates
CC (10(-3) to 10(-4)) of phase reversion, i.e. loss and regain of phiC31
CC resistance (PubMed:8446035, PubMed:12867465). When the pglW-pglX-pglY-
CC pglZ genes are transformed into a susceptible S.lividans (strain 1326)
CC they confer resistance to infection by phage phiC31 and phiBT1; all 4
CC genes are necessary (PubMed:11972785). {ECO:0000269|PubMed:11972785,
CC ECO:0000269|PubMed:12867465, ECO:0000269|PubMed:25592393,
CC ECO:0000269|PubMed:8446035, ECO:0000305|PubMed:11972785,
CC ECO:0000305|PubMed:25452498}.
CC -!- FUNCTION: Probably a toxic component of a type II toxin-antitoxin (TA)
CC system. The toxic activity is inhibited by its cognate antitoxin PglZ.
CC {ECO:0000269|PubMed:25592393}.
CC -!- FUNCTION: May be a subtypes G and alpha restriction enzyme that
CC recognizes and cleaves an unknown sequence. Methylates an adenine
CC residue in the same sequence. {ECO:0000303|PubMed:12654995}.
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:25592393};
CC -!- INDUCTION: Constitutively expressed, probably part of a pglW-pglX
CC operon. {ECO:0000269|PubMed:11972785}.
CC -!- DISRUPTION PHENOTYPE: Strain is no longer resistant to plaque formation
CC by bacteriophage phiC31 (a Pgl- phenotype).
CC {ECO:0000269|PubMed:11972785, ECO:0000269|PubMed:25592393}.
CC -!- MISCELLANEOUS: Phase reversion of this Pgl system is due in part to the
CC expansion and contraction of an 8-base long guanine tract in this
CC protein (corresponding to residues 259-263). The tract has been
CC observed to be 7, 8 and 9 nucleotides long in different derivatives; a
CC 7-G tract yields a 282 residue and the 9-G tract a 336 residue missense
CC protein. {ECO:0000269|PubMed:12867465}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PglX adenine
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AL939128; CAD55384.1; -; Genomic_DNA.
DR PIR; T29133; T29133.
DR PIR; T35036; T35036.
DR RefSeq; NP_733709.1; NC_003888.3.
DR RefSeq; WP_011031053.1; NZ_VNID01000002.1.
DR AlphaFoldDB; Q8CJM2; -.
DR STRING; 100226.SCO6627; -.
DR REBASE; 17310; ScoA3ORF6627P.
DR GeneID; 1102066; -.
DR KEGG; sco:SCO6627; -.
DR PATRIC; fig|100226.15.peg.6735; -.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_269467_0_0_11; -.
DR InParanoid; Q8CJM2; -.
DR PhylomeDB; Q8CJM2; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; DNA-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Toxin-antitoxin system; Transferase.
FT CHAIN 1..1210
FT /note="Adenine-specific methyltransferase PglX"
FT /id="PRO_0000452165"
FT REGION 1181..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 381
FT /note="Y->A: Does not restore phage resistance to a
FT deletion mutant, very little DNA methylation occurs in
FT vitro."
FT /evidence="ECO:0000269|PubMed:25592393"
SQ SEQUENCE 1210 AA; 136254 MW; 9CBEEE2FFD5F6F90 CRC64;
MIDRKALLND LKQQVKAVEA DLGKQVKALD EVGARLRAEY DQARKLGRTA ATWNSWLDER
VTQVAVAWVL GTVFVRFCED NRLIPEPYVT GPDNYRRDLA ETRYDVYVEA DDDPTYRGWL
RRAFAELGDG QAGRLLFDSD HNPLYQIPLS HDGARELVEF WRQRDEEGAL VHDFTDPLSA
DGTEGWGTRF LGDLYQDLSE AARKTYALLQ TPEFVEEFIL DRTMNPAVRE FGYEELKMID
PTCGSGHFVL GAFRRLVRLG GENQPGKDVH QRVRAALDSV HGVDINPFAV AIARFRLLVA
AMAASGVRTL DEASKYEWPV HLAVGDSLIK SGSQQGSLFG ESDDDLTDEL AEFKYATEDV
GEHPEMLRPG RYHVVVGNPP YITVKDKSLN ALYRELYPAC AGKYALSVPF AQRFFELAKR
EDAEGSGYGM VGQITANSFM KREFGTKLIE GYFGHAVELT EVIDTSGAYI PGHGTPTVIL
VGTRRGGDGR SPVIRTVRSV QGEPVAPENA EEGLVWRAIV EQIDKPGSVS QWVSVDDLDR
EKYFSKQPWV LADGGQEMLE QINAASHAIL KRDLHRIGFY GIMGADDAMS AVPRTFRRNN
AESEYVRRLV VGDEVRDFRI ADGDDAFHPY GSQRDLVGPD AFPNLAAWLW PYRTELGGRA
TFSGGTYFAD GRPWWEWHQL PKDVGAHAWS LNFAFVATHN HVVLDRSGCA FTRTAPVIKL
REGASEEEHL RLLGLLNSST AGFWLKMVSY PKGGDPVGDE GARVSVHPWS DRYEFTGTKL
QEFPLPSEYP TGLGTALDAL AQRLAAASPA AVAAEAVPIA GLLREARTRW EAIRSRMIAL
QEEMDWQVYS LYKLHSEDLR VSEDPDDTNI PELTLGGRAF EIVLARRVAA GEASDEWFKR
HNSTPITEIP AHWPAPYREI VQKRIDAIES NRAIGMVERP EYKRRWATEG WDALQEKALR
SWLLDRMENR DLWCDENGQP TILTLARLTD ALSRDEDFAS VAKLYAPRKE LAKVVAELIT
DEHVPFLSAL RYKPSGLKKR ADWEEVWDLQ RKEDAAPDEP AKRKIRDSIP VPPKYTSADF
LRPSYWKARG KLDVPKERFV SYGQTNAATP ELYGWAGWDH REQAQALATY FTNTALSTKE
ITPFLAGLLE LQPWLSQWHN EFDMLYSGSP ADFFAGYRQQ KQGEHGLTDD DLRGWRPPAA
TRRRRAAAKQ
