PGLZ_STRCO
ID PGLZ_STRCO Reviewed; 974 AA.
AC O86683; Q53943;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Alkaline phosphatase-like protein PglZ;
DE AltName: Full=Bacteriophage (PhiC31) resistance gene PglZ {ECO:0000303|PubMed:7642495};
DE AltName: Full=ORF2 {ECO:0000303|PubMed:7642495};
GN Name=pglZ {ECO:0000303|PubMed:7642495};
GN OrderedLocusNames=SCO6636 {ECO:0000312|EMBL:CAA20547.1};
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 IDENTIFICATION BY MASS SPECTROMETRY, AND POSSIBLE POST-TRANSLATIONAL
RP MODIFICATION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12421300; DOI=10.1046/j.1365-2958.2002.03219.x;
RA Hesketh A.R., Chandra G., Shaw A.D., Rowland J.J., Kell D.B., Bibb M.J.,
RA Chater K.F.;
RT "Primary and secondary metabolism, and post-translational protein
RT modifications, as portrayed by proteomic analysis of Streptomyces
RT coelicolor.";
RL Mol. Microbiol. 46:917-932(2002).
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 IN A TOXIN-ANTITOXIN SYSTEM, DOMAIN, AND MUTAGENESIS OF ASP-535;
RP ASP-694 AND 835-LYS--GLY-974.
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). The system undergoes high
CC rates (10(-3) to 10(-4)) of phase reversion, i.e. loss and regain of
CC phiC31 resistance (PubMed:8446035). When the pglW-pglX-pglY-pglZ genes
CC are 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). {ECO:0000269|PubMed:11972785,
CC ECO:0000269|PubMed:7642495, ECO:0000269|PubMed:8446035,
CC ECO:0000305|PubMed:25452498}.
CC -!- FUNCTION: Probably an antitoxin component of a type II toxin-antitoxin
CC (TA) system. Inhibits the toxic activity of its cognate toxin PglX.
CC {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 -!- DOMAIN: Deletion of the C-terminus (residues 835-974) still allows this
CC protein confer phage resistance and act as an antitoxin to PglX.
CC {ECO:0000269|PubMed:25592393}.
CC -!- PTM: Identified by mass spectrometry as a slightly larger than expected
CC protein, suggesting it may be modifed with a low molecular weight
CC adduct. {ECO:0000269|PubMed:12421300}.
CC -!- DISRUPTION PHENOTYPE: Strain is no longer resistant to plaque formation
CC by bacteriophage phiC31 (a Pgl- phenotype).
CC {ECO:0000269|PubMed:7642495}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; L37531; AAB00366.1; -; Genomic_DNA.
DR EMBL; AL939128; CAA20547.1; -; Genomic_DNA.
DR PIR; T30204; T30204.
DR PIR; T35045; T35045.
DR RefSeq; NP_630712.1; NC_003888.3.
DR RefSeq; WP_011031062.1; NZ_VNID01000002.1.
DR AlphaFoldDB; O86683; -.
DR STRING; 100226.SCO6636; -.
DR GeneID; 1102075; -.
DR KEGG; sco:SCO6636; -.
DR PATRIC; fig|100226.15.peg.6741; -.
DR eggNOG; COG1524; Bacteria.
DR HOGENOM; CLU_330036_0_0_11; -.
DR OMA; WDADSRY; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR013973; PglZ_dom.
DR Pfam; PF08665; PglZ; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..974
FT /note="Alkaline phosphatase-like protein PglZ"
FT /id="PRO_0000452168"
FT REGION 835..974
FT /note="Not necessary for Pgl+ phenotype or antitoxin
FT activity"
FT /evidence="ECO:0000269|PubMed:25592393"
FT MUTAGEN 535
FT /note="D->A: Does not complement Pgl- phenotype of C-
FT terminally shortened protein."
FT /evidence="ECO:0000269|PubMed:25592393"
FT MUTAGEN 694
FT /note="D->A: Does not complement Pgl- phenotype of C-
FT terminally shortened protein."
FT /evidence="ECO:0000269|PubMed:25592393"
FT MUTAGEN 835..974
FT /note="Missing: Shortened protein, still complements a pglZ
FT deletion and has antitoxin activity."
FT /evidence="ECO:0000269|PubMed:25592393"
FT CONFLICT 250..261
FT /note="LVDAERGEDAAA -> HARRRARRGRRR (in Ref. 1; AAB00366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 974 AA; 104124 MW; 9D4F539EBDDBB247 CRC64;
MTDTTVAVPG AVRLNTATVT QYLSSQSSLV ASLTGDGGGR RRAVLLRSAP QWDGPAEPAW
GEGRTAGIAV APSPLAVHEL VLDHLAARRP GPPVLVVLTD REQHELDPAI LARVHKLRID
TVDGWDVVRE AFGARQIDPR LKDVNWAAEA LLDATPPGSW PAVPGGWLSR QYALTALAQR
RLRLGRYDTE GGPRRPGDDR LDAQALLHWS TRPGAPERLL TLRGPERAGL TAFLGEEDQA
GLAGRTLLAL VDAERGEDAA AFGLVCAALW QHAEPAPETY RARGRAERYF GDRPPATGDQ
LDALVTVFGR ATEEHVTTLL AAGHRTAGTD ADQAREARRT TGTVLDRAAA LARQFGAEEA
VAASPVLRGG LEARFTAVGR ALAAGDTTAV ADAVRRLENH RLAAEPEESA RIERARMGQR
LARWLATDPP TDALTVADAL RRHVAETGWA DLALEHIEAG GDQGPVLKAA YDTLGTRVRD
RRRQIDASFA RSLAAWTQSG TQPGSMLTVE TFLDRVVGPL VRRGEERRTL MLVLDGMSAA
IANELGEELR RSWAEFDPLP EGDTPYRRAM AAALPTVTAV SRTSLFAGTL TKGTQADEKR
LFPALKLWGG APAAVFHKDD LRTETAGETF GPALTEALAD GRTHVAVVLN AIDDRLAKEQ
KLGDGAWRID DVPGLRDLLR VAATQGMAVV LTSDHGHVVD RHGTKVDPAA APESARHRLI
GGGPLAEREI TLSGPRVIWP EPGASIVALW DADSRYTALK AGYHGGASLA EVTIPALAFL
PFGAEPPKGW RELGDQRPVW WAPEETGKAP LPDEYTARPV AATASAPKKP TAKAKKDQAE
VARMHHGALF DVALTTEGDD ALLTPTVVSR TETLVTALLD SETYQAQLGG LARKPQQEQV
HKALTTLLDS GGTLPVTALA QRVGMPVTRG VGFAAVLGQL LNYDGVQVLE TLPDGRTLRL
HAALLREQFA LGAG
