ID   PGLZ_BACCH              Reviewed;         854 AA.
AC   P0DUF4;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Alkaline phosphatase-like protein PglZ {ECO:0000303|PubMed:25452498};
DE   AltName: Full=BREX protein PglZ {ECO:0000303|PubMed:25452498};
GN   Name=pglZ {ECO:0000303|PubMed:25452498}; ORFNames=BCH308197_0967;
OS   Bacillus cereus (strain H3081.97).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=451708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3081.97;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus H3081.97.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN ANTIVIRAL DEFENSE, INDUCTION, AND CLASSIFICATION AND
RP   NOMENCLATURE.
RC   STRAIN=H3081.97;
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).
CC   -!- FUNCTION: BREX systems (bacteriophage exclusion) provide immunity
CC       against bacteriophage. A core protein of a type 1 BREX system. This
CC       system allows phage adsorption but prevents phage DNA replication,
CC       without degradation of the phage DNA. Methylation of bacterial DNA by
CC       PglX probably guides self/non-self discrimination. When the brxA-brxB-
CC       brxC-pglX and pglZ-brxL operons are transformed into a susceptible
CC       B.subtilis strain (BEST7003) they confer resistance to bacteriophages
CC       SPbeta, SP16, Zeta, phi3T and SP02 and partial protection to phages
CC       SP01 and SP82G (these include lytic and temperate phage). They do not
CC       protect against phages phi105, rho10 or rho14. Additionally confers a
CC       very slight reduction in efficiency of plasmid transformation.
CC       {ECO:0000269|PubMed:25452498}.
CC   -!- INDUCTION: Part of the pglZ-brxL operon. {ECO:0000269|PubMed:25452498}.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; ABDL02000007; EDZ57605.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DUF4; -.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR014060; PglZ.
DR   InterPro; IPR013973; PglZ_dom.
DR   Pfam; PF08665; PglZ; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   TIGRFAMs; TIGR02687; TIGR02687; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense.
FT   CHAIN           1..854
FT                   /note="Alkaline phosphatase-like protein PglZ"
FT                   /id="PRO_0000452166"
SQ   SEQUENCE   854 AA;  99356 MW;  93A5AB2AFEA20420 CRC64;
     MNTKEINRVL QDTFNKELTE GKKRHIVFWY DEAGEFIEDI DELNLEGVRI WKLTPHNMFA
     TKLEVEKNDV NSNFLIYANM AKPSAREDWL LDVYKYSQEF ATDKMTVMMR ELGITNDAAL
     RDVFKKYTKF FKSKEREALF KSFSVPEYTE EQIDLVVLAS LCKCNIVNLD EVIKALFREQ
     LKETNKYWEN IRKFGNEETF WNLVEKTYGY NLQDKSINSL LIFFLLTNVS ETLSGDIPKT
     WQPYISAIPM NAIVFMNQFM NHSADEVIYN ELANTVEKQV KVTEHLQSKE IKDYITSDTF
     CCFDTNIITY ITKQLMNAIH DYTSYIEIIA ARRKLHWFSV FRNEYEALYQ AIQLFQQIYE
     MGNAITESQP FDLFKAYESK YHNIDTAYRK FYVAFDQIED KDGFRALRDK VENIYTNVYI
     NDLAIKWSDA LEGEQEEYWP IAGLESQHTF YRSFVQPFVN KEERVFVIIS DALRYEVAKE
     LSNMLNVERK ASTDIVAMQG VLPSYTDLGM ATLLPYKSIT FNENAEVYVN DYKASSTENR
     ATILSKHYKD STAIQYKDLA AMNRQQFRDV FSGKKVSYIY HNVIDARGDH AATEHEVFHA
     VEQTLKDIRS LVDQLINTVS ASNIVITADH GFIYNRDTLQ ASDKVKKDFL NTDIEKRRFI
     ISSESNSIEG TMNFSMDYVL GEGSGKYVKV PRGANRFAVQ GTGANYVHGG AMLQEIVVPV
     IKFKNDRSKS SKNDVRKVEV KLTSLTRKIT NSITYLEFFQ TEKIEGKKTP LRLKVYFTDE
     EGNRISNENI IIADSQSSKP EDRTFKEKFV LKSMTYDKTK KYYLVLEDEE EAVENIYEKV
     AFPIDIAITN DFGF