EATX_STRPY
ID EATX_STRPY Reviewed; 90 AA.
AC Q57231; Q6UZC8;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Antitoxin epsilon;
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).
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 ZETA TOXIN AND UNAG,
RP EXPRESSION IN E.COLI, AND FUNCTION AS AN ANTITOXIN.
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: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Neutralizes the toxic effect of cognate zeta toxin. Part of a
CC postsegregational killing (PSK) system involved in the killing of
CC plasmid-free cells. Continuous synthesis of the epsilon antitoxin is
CC required to counteract the zeta toxin. {ECO:0000269|Ref.7}.
CC -!- SUBUNIT: In the presence of the zeta toxin, forms an inactive
CC PezA(2)PezT(2) heterotetramer. The heterotetramer is still able to bind
CC the zeta toxin substrate UNAG. {ECO:0000269|Ref.7}.
CC -!- INTERACTION:
CC Q57231; Q54944; NbExp=4; IntAct=EBI-6407271, EBI-6407265;
CC -!- MISCELLANEOUS: Has a short half-life in vivo.
CC -!- SIMILARITY: Belongs to the epsilon antitoxin 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; CAA45933.1; -; Genomic_DNA.
DR EMBL; AY357120; AAR27198.1; -; Genomic_DNA.
DR EMBL; X66468; CAA47089.1; -; Genomic_DNA.
DR EMBL; X66468; CAA47090.1; -; Genomic_DNA.
DR EMBL; AY357120; AAR27201.1; -; Genomic_DNA.
DR PIR; S45083; S45083.
DR RefSeq; WP_000301765.1; NZ_WXZG01000017.1.
DR RefSeq; YP_232737.1; NC_006978.1.
DR RefSeq; YP_232742.1; NC_006978.1.
DR RefSeq; YP_232758.1; NC_006979.1.
DR RefSeq; YP_232763.1; NC_006979.1.
DR PDB; 1GVN; X-ray; 1.95 A; A/C=1-90.
DR PDB; 3Q8X; X-ray; 2.70 A; A/C=1-90.
DR PDBsum; 1GVN; -.
DR PDBsum; 3Q8X; -.
DR AlphaFoldDB; Q57231; -.
DR SMR; Q57231; -.
DR DIP; DIP-58968N; -.
DR IntAct; Q57231; 1.
DR GeneID; 8149052; -.
DR EvolutionaryTrace; Q57231; -.
DR GO; GO:0015643; F:toxic substance binding; IEA:InterPro.
DR GO; GO:0031342; P:negative regulation of cell killing; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IEA:InterPro.
DR Gene3D; 1.10.8.130; -; 1.
DR InterPro; IPR035569; Antitoxin_epsilon/PezA_dom_sf.
DR InterPro; IPR015090; Epsilon_antitox.
DR Pfam; PF08998; Epsilon_antitox; 1.
DR SUPFAM; SSF81710; SSF81710; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Plasmid; Toxin-antitoxin system.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12530535"
FT CHAIN 2..90
FT /note="Antitoxin epsilon"
FT /id="PRO_0000221550"
FT HELIX 5..31
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1GVN"
FT HELIX 63..83
FT /evidence="ECO:0007829|PDB:1GVN"
SQ SEQUENCE 90 AA; 10721 MW; 31628C7F2FDE4B50 CRC64;
MAVTYEKTFE IEIINELSAS VYNRVLNYVL NHELNKNDSQ LLEVNLLNQL KLAKRVNLFD
YSLEELQAVH EYWRSMNRYS KQVLNKEKVA
