PEZT_STRPN
ID PEZT_STRPN Reviewed; 253 AA.
AC Q97QZ1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Toxin PezT;
DE AltName: Full=UDP-N-acetylglucosamine kinase;
DE Short=UNAG kinase;
DE EC=2.7.1.176;
DE AltName: Full=Zeta toxin;
GN Name=pezT; OrderedLocusNames=SP_1051;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP DISRUPTION PHENOTYPE, AND OPERON STRUCTURE.
RC STRAIN=0100993 / NCIMB 40794 / Serotype 3;
RX PubMed=14977965; DOI=10.1128/iai.72.3.1587-1593.2004;
RA Brown J.S., Gilliland S.M., Spratt B.G., Holden D.W.;
RT "A locus contained within a variable region of pneumococcal pathogenicity
RT island 1 contributes to virulence in mice.";
RL Infect. Immun. 72:1587-1593(2004).
RN [3]
RP SUBUNIT, AND COMPLEX STABILITY.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=20442221; DOI=10.1074/jbc.m110.126250;
RA Mutschler H., Reinstein J., Meinhart A.;
RT "Assembly dynamics and stability of the pneumococcal epsilon zeta antitoxin
RT toxin (PezAT) system from Streptococcus pneumoniae.";
RL J. Biol. Chem. 285:21797-21806(2010).
RN [4]
RP EXPRESSION IN E.COLI, FUNCTION AS A UNAG KINASE, AND MUTAGENESIS OF
RP 243-GLY--LYS-253.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=21445328; 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), EXPRESSION IN E.COLI, FUNCTION AS A
RP TOXIN, FUNCTION AS A TRANSCRIPTIONAL COREPRESSOR, SUBUNIT, OPERON
RP STRUCTURE, AND MUTAGENESIS OF LYS-45; ASP-66; THR-117; THR-120; ARG-157 AND
RP ARG-170.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=17488720; DOI=10.1074/jbc.m701703200;
RA Khoo S.K., Loll B., Chan W.T., Shoeman R.L., Ngoo L., Yeo C.C.,
RA Meinhart A.;
RT "Molecular and structural characterization of the PezAT chromosomal toxin-
RT antitoxin system of the human pathogen Streptococcus pneumoniae.";
RL J. Biol. Chem. 282:19606-19618(2007).
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. Upon expression in E.coli results in decreased cell
CC growth and viability, followed 3 hours later by growth restoration; the
CC toxic effect and phosphorylation of UNAG are neutralized by
CC coexpression with cognate antitoxin PezA. A mutant lacking the last 11
CC residues is stably maintained in E.coli, unlike the wild-type which
CC undergoes spontaneous mutation. Expression of the deletion mutant in
CC rapidly growing liquid cultures leads to cell bulging, permeabilization
CC and massive lysis by 1 hour. Cells that survive are not able to undergo
CC cytokinesis. Expression in slowly growing cells leads to bulging but
CC not lysis.
CC -!- FUNCTION: Acts as a corepressor of its own operon with PezA; it is not
CC clear if it binds DNA alone.
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: Forms a PezA(2)PezT(2) heterotetramer. The heterotetramer is
CC much more stable than either of the proteins alone, and a specific
CC mechanism may be necessary to liberate the toxin.
CC {ECO:0000269|PubMed:17488720, ECO:0000269|PubMed:20442221}.
CC -!- INDUCTION: Conflicting data is available; found to be a member of the
CC pezAT operon (upon ectopic expression in E.coli); in S.pneumoniae
CC strain 0100993 is found in an operon with the 2 following genes
CC (SP_1052 and SP_1053).
CC -!- DISRUPTION PHENOTYPE: Strains with a pezT/SP_1052/SP_1053 disruption
CC have partially attenuated virulence, they take longer to develop a
CC terminal infection in mice, although they grow normally in liquid
CC culture. A double SP_1052/SP_1053 disruption grows almost as well as
CC wild-type, showing the effect is mostly due to disruption of pezT.
CC {ECO:0000269|PubMed:14977965}.
CC -!- SIMILARITY: Belongs to the zeta toxin family. {ECO:0000305}.
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DR EMBL; AE005672; AAK75165.1; -; Genomic_DNA.
DR PIR; D95121; D95121.
DR RefSeq; WP_000405360.1; NZ_AKVY01000001.1.
DR PDB; 2P5T; X-ray; 3.20 A; B/D/F/H=1-253.
DR PDBsum; 2P5T; -.
DR AlphaFoldDB; Q97QZ1; -.
DR SMR; Q97QZ1; -.
DR DIP; DIP-58971N; -.
DR IntAct; Q97QZ1; 1.
DR STRING; 170187.SP_1051; -.
DR EnsemblBacteria; AAK75165; AAK75165; SP_1051.
DR KEGG; spn:SP_1051; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; QECLFGK; -.
DR PhylomeDB; Q97QZ1; -.
DR BioCyc; SPNE170187:G1FZB-1080-MON; -.
DR BRENDA; 2.7.1.176; 1960.
DR EvolutionaryTrace; Q97QZ1; -.
DR Proteomes; UP000000585; Chromosome.
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; Kinase; Nucleotide-binding; Repressor;
KW Toxin-antitoxin system; Transferase; Virulence.
FT CHAIN 1..253
FT /note="Toxin PezT"
FT /id="PRO_0000410967"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17488720"
FT MUTAGEN 45
FT /note="K->A: Abolishes lethality."
FT /evidence="ECO:0000269|PubMed:17488720"
FT MUTAGEN 66
FT /note="D->T: Abolishes lethality."
FT /evidence="ECO:0000269|PubMed:17488720"
FT MUTAGEN 117
FT /note="T->V: Abolishes lethality."
FT /evidence="ECO:0000269|PubMed:17488720"
FT MUTAGEN 120
FT /note="T->V: Very slight reduction in toxic effect."
FT /evidence="ECO:0000269|PubMed:17488720"
FT MUTAGEN 157
FT /note="R->A: Abolishes lethality."
FT /evidence="ECO:0000269|PubMed:17488720"
FT MUTAGEN 170
FT /note="R->A: Abolishes lethality."
FT /evidence="ECO:0000269|PubMed:17488720"
FT MUTAGEN 243..253
FT /note="Missing: Retains toxicity while being stably
FT maintained in E.coli."
FT /evidence="ECO:0000269|PubMed:21445328"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:2P5T"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:2P5T"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2P5T"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 87..107
FT /evidence="ECO:0007829|PDB:2P5T"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:2P5T"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:2P5T"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:2P5T"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2P5T"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2P5T"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:2P5T"
SQ SEQUENCE 253 AA; 29129 MW; 0F7CD8D0B26EE89E CRC64;
MEIQDYTDSE FKHALARNLR SLTRGKKSSK QPIAILLGGQ SGAGKTTIHR IKQKEFQGNI
VIIDGDSFRS QHPHYLELQQ EYGKDSVEYT KDFAGKMVES LVTKLSSLRY NLLIEGTLRT
VDVPKKTAQL LKNKGYEVQL ALIATKPELS YLSTLIRYEE LYIINPNQAR ATPKEHHDFI
VNHLVDNTRK LEELAIFERI QIYQRDRSCV YDSKENTTSA ADVLQELLFG EWSQVEKEML
QVGEKRLNEL LEK
