ID   ZTOX_ENTHR              Reviewed;         286 AA.
AC   Q93CM1;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, 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 hirae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12195739; DOI=10.1078/1438-4221-00194;
RA   Werner G., Klare I., Witte W.;
RT   "Molecular analysis of streptogramin resistance in enterococci.";
RL   Int. J. Med. Microbiol. 292:81-94(2002).
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 cognate epsilon
CC       antitoxin. Part of a postsegregational killing (PSK) system involved in
CC       the killing of plasmid-free cells. The zeta toxin induces programmed
CC       cell 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF406971; AAK96239.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93CM1; -.
DR   SMR; Q93CM1; -.
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..286
FT                   /note="Toxin zeta"
FT                   /id="PRO_0000221552"
FT   REGION          249..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..286
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97QZ1"
SQ   SEQUENCE   286 AA;  32421 MW;  0AF3FBE7974B0F92 CRC64;
     MRLHKIFYAL FENRLSDNLE ELVQGKKAVE SPTAFLLGGQ PGSGKTSLRS AIFEETQGNV
     IVIDNDTFKQ QHPNFDELVK LYEKDVVKHV TPYSNRMTEA IISRLSDKGY NLVIEGTGRT
     TDVPIQTATM LQAKGYETKM YVMAVPKINS YLGTIERYET MYADDPMTAR ATPKQAHDIA
     VKNLPTNLET LHKTGLFSDI RLYNREGVKL YSSLETPSIS PKETLERELN RKISGKEIQP
     TLERIEQKMV QNQHQETPEF KAIQQKMESL QPPTPPIPKT PKLPGI