ID   ZTOX_ENTFL              Reviewed;         287 AA.
AC   P0A4M1; Q9AL18;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Toxin zeta;
DE   AltName: Full=UDP-N-acetylglucosamine kinase;
DE            Short=UNAG kinase;
DE            EC=2.7.1.176;
OS   Enterococcus faecalis (Streptococcus faecalis).
OG   Plasmid pRE25.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RE25;
RX   PubMed=11735367; DOI=10.1006/plas.2001.1544;
RA   Schwarz F.V., Perreten V., Teuber M.;
RT   "Sequence of the 50-kb conjugative multiresistance plasmid pRE25 from
RT   Enterococcus faecalis RE25.";
RL   Plasmid 46:170-187(2001).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC       Phosphorylates UDP-N-acetyl-D-glucosamine (UNAG) on the 3'-hydroxyl
CC       group of the N-acetyl-D-glucosamine moiety, yielding UNAG-3P. UNAG-3P
CC       inhibits MurA, the first committed step in cell wall synthesis, which
CC       is then blocked. Phosphorylation is inhibited by epsilon antitoxin.
CC       Part of a postsegregational killing (PSK) system involved in the
CC       killing of plasmid-free cells. The zeta toxin induces programmed cell
CC       death (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + UDP-N-acetyl-alpha-D-glucosamine = ADP + H(+) + UDP-N-
CC         acetyl-alpha-D-glucosamine 3'-phosphate; Xref=Rhea:RHEA:32671,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:64353, ChEBI:CHEBI:456216; EC=2.7.1.176;
CC   -!- SUBUNIT: In the presence of the epsilon antitoxin, forms an inactive
CC       PezA(2)PezT(2) heterotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zeta toxin family. {ECO:0000305}.
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DR   EMBL; X92945; CAC29174.1; -; Genomic_DNA.
DR   RefSeq; WP_002332783.1; NZ_VWOE01000025.1.
DR   RefSeq; YP_783903.1; NC_008445.1.
DR   AlphaFoldDB; P0A4M1; -.
DR   SMR; P0A4M1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010488; Zeta_toxin_domain.
DR   Pfam; PF06414; Zeta_toxin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Plasmid; Toxin-antitoxin system;
KW   Transferase.
FT   CHAIN           1..287
FT                   /note="Toxin zeta"
FT                   /id="PRO_0000221551"
FT   REGION          250..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..287
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97QZ1"
SQ   SEQUENCE   287 AA;  32675 MW;  ACF044DAD87E9DC1 CRC64;
     MANITDFTEK QFEDRLEKNV ERLTKNRLAV ESPTAFLLGG QPGSGKTSLR SAISEETQGN
     VVIIDNDTFK QQHPNFDELV KLYEKDVVKY VTPYSNRMTE AIISRLRDKG YNLVIEGTGR
     TTDVPIQTAT MLQAKDYETK MYVMAVPKIN SYLGTIERYE TMYADDPMTA RATPKQAHDI
     VVKNLPTNLE TLHKTGLFSD IRLYNREGVK LYSSLETPSI SPKETLEREL NRKVSGKEIQ
     PTLERIEQKM VQNQHQETPE FKAIQQKMES LQPPTPPIPK TPKLPGI