PGLW_STRCO
ID PGLW_STRCO Reviewed; 1557 AA.
AC O86560;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable kinase PglW {ECO:0000303|PubMed:11972785};
DE AltName: Full=Bacteriophage (PhiC31) resistance gene PglW {ECO:0000303|PubMed:11972785};
GN Name=pglW {ECO:0000303|PubMed:11972785}; Synonyms=SC1F2.23;
GN OrderedLocusNames=SCO6626;
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 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 [5]
RP FUNCTION AS A KINASE, AND MUTAGENESIS OF LYS-677.
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 (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). When the pglW-pglX-pglY-pglZ genes are
CC transformed into a susceptible S.lividans (strain 1326) they confer
CC resistance to infection by phage phiC31 and phiBT1; all 4 genes are
CC necessary (PubMed:11972785). The proteins has kinase domains and might
CC bind DNA (Probable). {ECO:0000269|PubMed:11972785,
CC ECO:0000269|PubMed:8446035, ECO:0000305|PubMed:11972785,
CC ECO:0000305|PubMed:25452498}.
CC -!- FUNCTION: Autophosphorylates when synthesized in vitro, cannot be
CC expressed in E.coli. {ECO:0000269|PubMed:25592393}.
CC -!- INDUCTION: Constitutively expressed, probably part of a pglW-pglX
CC operon. {ECO:0000269|PubMed:11972785}.
CC -!- DOMAIN: The first protein kinase domain is predicted to be
CC catalytically inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Strain is no longer resistant to plaque formation
CC by bacteriophage phiC31 (a Pgl- phenotype).
CC {ECO:0000269|PubMed:11972785}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AL939128; CAA20514.1; -; Genomic_DNA.
DR PIR; T29132; T29132.
DR RefSeq; NP_630703.1; NC_003888.3.
DR RefSeq; WP_011031052.1; NZ_VNID01000002.1.
DR AlphaFoldDB; O86560; -.
DR SMR; O86560; -.
DR STRING; 100226.SCO6626; -.
DR GeneID; 1102065; -.
DR KEGG; sco:SCO6626; -.
DR PATRIC; fig|100226.15.peg.6734; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_005315_0_0_11; -.
DR OMA; DDHAERY; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011528; NERD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF08378; NERD; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50965; NERD; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..1557
FT /note="Probable kinase PglW"
FT /id="PRO_0000452169"
FT DOMAIN 12..130
FT /note="NERD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00327"
FT DOMAIN 195..490
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 530..816
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 615..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 536..544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 677
FT /note="K->A: Does not complement the Pgl- phenotype of a
FT deletion mutation, does not autophosphorylate."
FT /evidence="ECO:0000269|PubMed:25592393"
SQ SEQUENCE 1557 AA; 169204 MW; D53E18C3BE28392E CRC64;
MREGRWVTVT ESEFEHERRG LEAIRQKLPD GDPWRAWSNF TFTANTGHVR EVDLLVVAPG
GLCMVELKDW HGSVTSENGT WVQTTPGGRR RTHGNPLHLV NRKAKELAGL LAQPGAKRVW
VAEAVCFTDN GLRVRLPAHD QNGVYTVDEL VDMLKQAPSD ERRRVTAIGS REVAAALKNI
GIRKSDAQYK VGPYELERKS FDSGPTWADY LARHSDLPEA ARVRIYLSER GSDASLRQSV
ENAARREAAV LGRFKHPGAV QLKQYFPSGH AAGPALIFDY HPHTQKLDEY LVQYGEKLDI
LGRMALVRQL AETVRSAHAS RIHHRALAAR SVLVVPRSRG GKGRAVGEEA AWLTPQLQIS
DWQIATQRSG DSSQGQGMTR FAPTALSAMH LADDADAYLA PELTALNPDP VYLDVYGLGV
LTYLLVTGKA PAASQAELLA RLEAGEGLRP SSLVDGLSED VDELVQAATA YRPGQRLSSV
DEFLELLEVV EDSLTAPAAA LDGPAEDETG ASADKDPLEV VAGDLLAGRW EVRRRLGTGS
TSRAFLVRDL EAETRRTRPL AVLKVALSDS RGEILVREAE AMRRLRPHSG IIRLAEPEPL
HIGGRTVLAL EYVGDERDDD GPGAEGATRP RRREETVARQ LREHGRLPVD QLEAYGDYLF
GAVDFLEGEG IWHRDIKPDN IAVRIRPNRT RELVLIDFSL AGYPAKNTDA GTDGYLDPFV
DVITRGSYDS HAERYAVAVT LHQMASGELP KWGDGSVLPR MTDPKEWPYP TIAAEAFDPA
VRDGLVAFFQ KALHRDAGKR FPELKPMRDA WRKVFLDASQ TVPSSHRTRP AAPADGAAPA
EGAAAGIADA EPETAEQQRD RLAAEVTRDT PLTVSGLTPA AQSFLYGLGI TTVGELLDYS
RRKLVNAPGL GAKTRNEVQQ RQREWGERLR EAPVSPLTPK GRAEAKEELE QLTAAESALV
GQLATGESAG ALSARTLRSV SLDTLATVLV PAVNNNGSNR NKAEMVRLLL RLPDEHGVLP
GIGVWPKQKD VADALGLSHG RIPQMLKDER KRWKAEPAVQ ALRDEIIELL ASMGRVASAV
EIADALAVRR GTHLAGREQR RAMALAAVRA VVEVEQLVPQ EVEFQHQPNR KATDESLGAG
LLALDVREDD APDTPTAPGL LDYATRLGKT ADRLARLDTL PTAATVLAEL GALTVPPGAV
DWDERRMVEL AAAASVNAAA TPRLEIYPRD LSLVRALRLT QAGLVRWIPG VPEGRQPGLT
GEDVHERVRA RFPELVVPDG RGGTAHELPT AGPLTKALRD AGFELSLSMR EDTGTLRYLP
TRVDEASSYL TTGAWRQSTR TGTVTRYADD PQLAGAVRAE ERLLASAHRD GYRVLTVRQQ
LVRDAVRELG AERLGGQAVS VTELFLEALH GQVTPGTKPT WETLLKADAA EPGSKGAVRF
AEYARTAWGS VEPRIAELLG DGGGGAGPVL LTEAGVFARY DAMGVLDRLA SAARRGGRGL
WLLVPQSDPS REPRLGQVAV PYQAGLGEWI QLPDTWVGNR HRGSGEVVAS GVEGDAK
