PGLY_STRCO
ID PGLY_STRCO Reviewed; 1294 AA.
AC O86682; Q53942;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=ATPase PglY {ECO:0000303|PubMed:25592393};
DE AltName: Full=Bacteriophage (PhiC31) resistance gene PglY;
DE AltName: Full=ORF1 {ECO:0000303|PubMed:7642495};
GN Name=pglY {ECO:0000303|PubMed:7642495};
GN OrderedLocusNames=SCO6635 {ECO:0000312|EMBL:CAA20546.1};
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 [GENOMIC DNA], FUNCTION IN ANTIVIRAL DEFENSE,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=7642495; DOI=10.1128/jb.177.16.4681-4689.1995;
RA Bedford D.J., Laity C., Buttner M.J.;
RT "Two genes involved in the phase-variable phi C31 resistance mechanism of
RT Streptomyces coelicolor A3(2).";
RL J. Bacteriol. 177:4681-4689(1995).
RN [2]
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 [3]
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 [4]
RP FUNCTION IN ANTIVIRAL DEFENSE, AND DISRUPTION PHENOTYPE.
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 [5]
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 [6]
RP FUNCTION AS AN ATPASE, AND MUTAGENESIS OF 81-LYS-SER-82.
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 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 (PubMed:7642495) (Probable). The system
CC undergoes high rates (10(-3) to 10(-4)) of phase reversion, i.e. loss
CC and regain of phiC31 resistance (PubMed:8446035). When the pglW-pglX-
CC pglY-pglZ genes are transformed into a susceptible S.lividans (strain
CC 1326) they confer resistance to infection by phage phiC31 and phiBT1;
CC all 4 genes are necessary (PubMed:11972785).
CC {ECO:0000269|PubMed:11972785, ECO:0000269|PubMed:7642495,
CC ECO:0000269|PubMed:8446035, ECO:0000305|PubMed:11972785,
CC ECO:0000305|PubMed:25452498}.
CC -!- FUNCTION: Hydrolyzes ATP but not AMP, ADP, GMP, GDP or GTP; activity is
CC inhibited by the non-hydrolyzable ATP analog 5-adenylyl beta,gamma-
CC imidodiphosphate. {ECO:0000269|PubMed:25592393}.
CC -!- INDUCTION: Constitutively expressed, not induced by bacteriophage
CC phiC31, probably part of a pglY-pglZ operon.
CC {ECO:0000269|PubMed:7642495}.
CC -!- DISRUPTION PHENOTYPE: Strain is no longer resistant to plaque formation
CC by bacteriophage phiC31 (a Pgl- phenotype).
CC {ECO:0000269|PubMed:7642495}.
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DR EMBL; L37531; AAB00365.1; -; Genomic_DNA.
DR EMBL; AL939128; CAA20546.1; -; Genomic_DNA.
DR PIR; T35044; T35044.
DR RefSeq; NP_630711.1; NC_003888.3.
DR RefSeq; WP_011031061.1; NC_003888.3.
DR AlphaFoldDB; O86682; -.
DR STRING; 100226.SCO6635; -.
DR GeneID; 1102074; -.
DR KEGG; sco:SCO6635; -.
DR PATRIC; fig|100226.15.peg.6740; -.
DR eggNOG; COG1483; Bacteria.
DR HOGENOM; CLU_269246_0_0_11; -.
DR OMA; FLMVPYH; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antiviral defense; Reference proteome.
FT CHAIN 1..1294
FT /note="ATPase PglY"
FT /id="PRO_0000452161"
FT REGION 1205..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 81..82
FT /note="KS->AA: Does not restore phage resistance to a
FT deletion mutant, much less ATPase activity."
FT /evidence="ECO:0000269|PubMed:25592393"
FT CONFLICT 373
FT /note="K -> N (in Ref. 1; AAB00365)"
FT /evidence="ECO:0000305"
FT CONFLICT 914
FT /note="M -> I (in Ref. 1; AAB00365)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="E -> A (in Ref. 1; AAB00365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1294 AA; 141188 MW; 5515825E3087B4F1 CRC64;
MAQPPLLRDV IDIKESISTS DFVLSLAEAT TPAGAQHALR DYVVTERLLE NFDEALALIK
SSLDGHRSKA AYLHGSFGSG KSHFMAVLYA LLSGDQAARA RTEFDPVLTK HQWLSTDGKK
FLLVPYHMLG AKALEQRVLG GYVTHVKKLC PEAPTPQVYR TDSLFADIRA MRANMGDEAV
IRALGTSGAD DAEEDEWGEG FAWTPQLLDT ALAAEESHEA GVHLNLTNPS TPAELRAKLV
NDAGTNLLPG FTQNAAEDEH GFISLDAGLS VIAEHAKSLG YDGLILFMDE LILWLATLIH
DQKFVAREAS KITNFVEGGD ARRAIPVMSF IARQRDLREL VGEEVSGAAE SSIQDTLNLA
SGRFDKITLE DRKLPQIAHA RLLKPKDAEA AQQVDAAFEQ TKRVGPQVWD TLLGSEKGTT
GADAESFRLT YPFSPAFMDT LVHISSALQR SRTGLKLMGQ LLADHRDELR LGQLVPVGDL
YPVIAQGGDK PFTDSLKVVF EAADKLYKTK LRPYLLSSYD ITEDDVEQYR NRPESLTDPK
KLNGCRMFTG DNRLVCTLLL SALAPSVPAL SELTIRRLGA LNHGSVLAPI PGAEVGIIKN
KVAEWAARFP EIKETGTDAN PGVRLELSGV DVDSVIANAQ VNDNPGNRVA LARRLLSEEL
GVEHGQLSDQ LGFTWRGTAR TAEIVFGNVA DEDELPDHDL MPQEEGRWRI AIDLPFDEGE
WGPVEDVNRV QRLRERQQGE RSRTIAWLPA HLSATRFADF RRLVVIDKAL ADEHRFDTQY
AGHLNADNRS RAKGLLETQR EALLKQAKGA FKQAYGLAQK QAADVVPDFD DHLVALPDVD
GLTLSFGQSL HDGIRHVAGK LLTHQYPAHP DLDPDATGTA VKPADTKKVF AHVRAAAEAR
DGRIEVPAAD RKLMQRIAGP LRLGQQKEAY FELSRYWGDH FRQLARSQGV TGDLSLITLT
DWTDRPDPRG LPDFLARLVV AAFAEMDDRV WVRGGTVLDP APELAAIKDH DALRSQPLPA
ESDWDTARQR FETVFGAKPP ALRRGRMVNQ FARQIIEAAR DYRDHAADLV HQLEAHASFL
GLDQTADTGR LALARRSLQL LDALTAEAGK GAAGAKKTVE ALASFDLGET SADRYGTSIK
KARAVAEAVA SAPWSTLELA AGLGPEGEAL LDSLRNVARD DQRTADLRDA LARTQREVVA
LIKRTQAAAT PPPAPAASQP TAGDLSLDTP TSDPRIPYTS QETPTSSGGA GTARTSGGRR
TTAARAVTDL QAELSDLAVR HPEATIEITW RVVE
