PEZA_STRPN
ID PEZA_STRPN Reviewed; 158 AA.
AC Q97QZ2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Antitoxin PezA;
GN Name=pezA; OrderedLocusNames=SP_1050;
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 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 FUNCTION AS AN ANTITOXIN, AND EXPRESSION IN E.COLI.
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
RP AN ANTITOXIN, FUNCTION AS A TRANSCRIPTION REPRESSOR, SUBUNIT, DNA-BINDING,
RP AND OPERON STRUCTURE.
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: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Upon expression in E.coli neutralizes the toxic effect of cognate toxin
CC PezT. Represses transcription of its own operon, PezT acts as a
CC corepressor, considerably increasing repression.
CC {ECO:0000269|PubMed:17488720, ECO:0000269|PubMed:21445328}.
CC -!- SUBUNIT: Probably a homodimer, forms a PezA(2)PezT(2) heterotetramer.
CC The heterotetramer is much more stable than either of the proteins
CC alone, and a specific 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 a monocistronic operon.
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DR EMBL; AE005672; AAK75164.1; -; Genomic_DNA.
DR PIR; C95121; C95121.
DR RefSeq; WP_000579608.1; NZ_AKVY01000001.1.
DR PDB; 2P5T; X-ray; 3.20 A; A/C/E/G=1-158.
DR PDBsum; 2P5T; -.
DR AlphaFoldDB; Q97QZ2; -.
DR SMR; Q97QZ2; -.
DR DIP; DIP-58970N; -.
DR IntAct; Q97QZ2; 2.
DR STRING; 170187.SP_1050; -.
DR EnsemblBacteria; AAK75164; AAK75164; SP_1050.
DR KEGG; spn:SP_1050; -.
DR eggNOG; COG1396; Bacteria.
DR OMA; KEFAMIG; -.
DR PhylomeDB; Q97QZ2; -.
DR BioCyc; SPNE170187:G1FZB-1079-MON; -.
DR EvolutionaryTrace; Q97QZ2; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR Gene3D; 1.10.8.130; -; 1.
DR InterPro; IPR035569; Antitoxin_epsilon/PezA_dom_sf.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Repressor; Toxin-antitoxin system;
KW Transcription; Transcription regulation.
FT CHAIN 1..158
FT /note="Antitoxin PezA"
FT /id="PRO_0000410966"
FT DOMAIN 6..60
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 17..36
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT HELIX 69..98
FT /evidence="ECO:0007829|PDB:2P5T"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:2P5T"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2P5T"
FT HELIX 132..154
FT /evidence="ECO:0007829|PDB:2P5T"
SQ SEQUENCE 158 AA; 18248 MW; 0ABB5257446881C5 CRC64;
MIGKNIKSLR KTHDLTQLEF ARIVGISRNS LSRYENGTSS VSTELIDIIC QKFNVSYVDI
VGEDKMLNPV EDYELTLKIE IVKERGANLL SRLYRYQDSQ GISIDDESNP WILMSDDLSD
LIHTNIYLVE TFDEIERYSG YLDGIERMLE ISEKRMVA
