ZTOX_STRPY
ID ZTOX_STRPY Reviewed; 287 AA.
AC Q54944; Q54938; Q54939; Q6UZC4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Toxin zeta;
DE AltName: Full=UDP-N-acetylglucosamine kinase;
DE Short=UNAG kinase;
DE EC=2.7.1.176;
OS Streptococcus pyogenes.
OG Plasmid pBT233, and Plasmid pSM19035.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pBT233;
RX PubMed=8293991; DOI=10.1016/0378-1119(93)90441-5;
RA Ceglowski P., Boitsov A., Chai S., Alonso J.C.;
RT "Analysis of the stabilization system of pSM19035-derived plasmid pBT233 in
RT Bacillus subtilis.";
RL Gene 136:1-12(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pSM19035;
RX PubMed=8093174; DOI=10.1016/0378-1119(94)90319-0;
RA Ceglowski P., Alonso J.C.;
RT "Gene organization of the Streptococcus pyogenes plasmid pDB101: sequence
RT analysis of the orf eta-copS region.";
RL Gene 145:33-39(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pSM19035;
RA Kern-Zdanowicz I., Zienkiewicz M., Ceglowski P.;
RT "Nucleotide sequence of the small EcoRI fragment of Streptococcus pyogenes
RT plasmid pSM19035.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-10, AND CHARACTERIZATION.
RC PLASMID=pSM19035;
RX PubMed=12530535; DOI=10.1515/bc.2002.191;
RA Camacho A.G., Misselwitz R., Behlke J., Ayora S., Welfle K., Meinhart A.,
RA Lara B., Saenger W., Welfle H., Alonso J.C.;
RT "In vitro and in vivo stability of the epsilon2zeta2 protein complex of the
RT broad host-range Streptococcus pyogenes pSM19035 addiction system.";
RL Biol. Chem. 383:1701-1713(2002).
RN [5]
RP CRYSTALLIZATION.
RC PLASMID=pSM19035;
RX PubMed=11320325; DOI=10.1107/s0907444901004176;
RA Meinhart A., Alings C., Straeter N., Camacho A.G., Alonso J.C., Saenger W.;
RT "Crystallization and preliminary X-ray diffraction studies of the epsilon
RT zeta addiction system encoded by Streptococcus pyogenes plasmid pSM19035.";
RL Acta Crystallogr. D 57:745-747(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND MUTAGENESIS OF LYS-46; ASP-67;
RP ARG-158 AND ARG-171.
RC PLASMID=pSM19035;
RX PubMed=12571357; DOI=10.1073/pnas.0434325100;
RA Meinhart A., Alonso J.C., Straeter N., Saenger W.;
RT "Crystal structure of the plasmid maintenance system epsilon/zeta:
RT Functional mechanism of toxin zeta and inactivation by epsilon2zeta2
RT complex formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1661-1666(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH EPSILON ANTITOXIN AND
RP UNAG, EXPRESSION IN E.COLI, AND FUNCTION AS A UNAG KINASE.
RC PLASMID=pSM19035;
RX DOI=10.1371/journal.pbio.1001033;
RA Mutschler H., Gebhardt M., Shoeman R.L., Meinhart A.;
RT "A novel mechanism of programmed cell death in bacteria by toxin-antitoxin
RT systems corrupts peptidoglycan synthesis.";
RL PLoS Biol. 9:E1001033-E1001033(2011).
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. {ECO:0000269|Ref.7}.
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. The heterotetramer is still able to bind
CC the UNAG substrate. {ECO:0000269|Ref.7}.
CC -!- INTERACTION:
CC Q54944; Q57231; NbExp=4; IntAct=EBI-6407265, EBI-6407271;
CC -!- MISCELLANEOUS: Has a long half-life in vivo.
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; X64695; CAA45934.1; -; Genomic_DNA.
DR EMBL; AY357120; AAR27199.1; -; Genomic_DNA.
DR EMBL; X66468; CAA47091.1; -; Genomic_DNA.
DR EMBL; AY357120; AAR27200.1; -; Genomic_DNA.
DR EMBL; X66468; CAA47092.1; -; Genomic_DNA.
DR PIR; S45085; S45085.
DR RefSeq; WP_001284311.1; NZ_JABUAN010000008.1.
DR RefSeq; YP_232738.1; NC_006978.1.
DR RefSeq; YP_232741.1; NC_006978.1.
DR RefSeq; YP_232759.1; NC_006979.1.
DR RefSeq; YP_232762.1; NC_006979.1.
DR PDB; 1GVN; X-ray; 1.95 A; B/D=1-287.
DR PDB; 3Q8X; X-ray; 2.70 A; B/D=1-287.
DR PDBsum; 1GVN; -.
DR PDBsum; 3Q8X; -.
DR AlphaFoldDB; Q54944; -.
DR SMR; Q54944; -.
DR DIP; DIP-58969N; -.
DR IntAct; Q54944; 1.
DR GeneID; 8149053; -.
DR BRENDA; 2.7.1.176; 5935.
DR EvolutionaryTrace; Q54944; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Plasmid; Toxin-antitoxin system; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12530535"
FT CHAIN 2..287
FT /note="Toxin zeta"
FT /id="PRO_0000221554"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:12571357"
FT BINDING 66
FT /ligand="substrate"
FT BINDING 100
FT /ligand="substrate"
FT BINDING 118
FT /ligand="substrate"
FT BINDING 120
FT /ligand="substrate"
FT BINDING 128
FT /ligand="substrate"
FT MUTAGEN 46
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12571357"
FT MUTAGEN 67
FT /note="D->T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12571357"
FT MUTAGEN 158
FT /note="R->A: Loss of activity; when associated with S-171."
FT /evidence="ECO:0000269|PubMed:12571357"
FT MUTAGEN 171
FT /note="R->S: Loss of activity; when associated with A-158."
FT /evidence="ECO:0000269|PubMed:12571357"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:1GVN"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:1GVN"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1GVN"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 88..109
FT /evidence="ECO:0007829|PDB:1GVN"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:1GVN"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1GVN"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:1GVN"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 175..195
FT /evidence="ECO:0007829|PDB:1GVN"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1GVN"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1GVN"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 236..252
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:1GVN"
SQ SEQUENCE 287 AA; 32404 MW; B0C6282EE5B2210F CRC64;
MANIVNFTDK QFENRLNDNL EELIQGKKAV ESPTAFLLGG QPGSGKTSLR SAIFEETQGN
VIVIDNDTFK QQHPNFDELV KLYEKDVVKH VTPYSNRMTE AIISRLSDQG YNLVIEGTGR
TTDVPIQTAT MLQAKGYETK MYVMAVPKIN SYLGTIERYE TMYADDPMTA RATPKQAHDI
VVKNLPTNLE TLHKTGLFSD IRLYNREGVK LYSSLETPSI SPKETLEKEL NRKVSGKEIQ
PTLERIEQKM VLNKHQETPE FKAIQQKLES LQPPTPPIPK TPKLPGI
