MAZE_STAAE
ID MAZE_STAAE Reviewed; 56 AA.
AC P0C7B4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Antitoxin MazE;
GN Name=mazE; OrderedLocusNames=NWMN_1974.1;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP FUNCTION AS AN ANTITOXIN, INDUCTION, AND SUBUNIT.
RC STRAIN=Newman;
RX PubMed=17933891; DOI=10.1128/jb.01272-07;
RA Fu Z., Donegan N.P., Memmi G., Cheung A.L.;
RT "Characterization of mazFSa, an endoribonuclease from Staphylococcus
RT aureus.";
RL J. Bacteriol. 189:8871-8879(2007).
RN [3]
RP FUNCTION.
RC STRAIN=Newman;
RX PubMed=19168622; DOI=10.1128/jb.00907-08;
RA Fu Z., Tamber S., Memmi G., Donegan N.P., Cheung A.L.;
RT "Overexpression of MazFsa in Staphylococcus aureus induces bacteriostasis
RT by selectively targeting mRNAs for cleavage.";
RL J. Bacteriol. 191:2051-2059(2009).
RN [4]
RP FUNCTION.
RX PubMed=19251861; DOI=10.1128/jb.01815-08;
RA Zhu L., Inoue K., Yoshizumi S., Kobayashi H., Zhang Y., Ouyang M., Kato F.,
RA Sugai M., Inouye M.;
RT "Staphylococcus aureus MazF specifically cleaves a pentad sequence, UACAU,
RT which is unusually abundant in the mRNA for pathogenic adhesive factor
RT SraP.";
RL J. Bacteriol. 191:3248-3255(2009).
RN [5]
RP FUNCTION.
RC STRAIN=NRS26;
RX PubMed=23994560; DOI=10.1016/j.ab.2013.08.018;
RA van Rensburg J.J., Hergenrother P.J.;
RT "Detection of endogenous MazF enzymatic activity in Staphylococcus
RT aureus.";
RL Anal. Biochem. 443:81-87(2013).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Labile antitoxin that binds to cognate MazF toxin and counteracts its
CC endoribonuclease activity. {ECO:0000269|PubMed:17933891,
CC ECO:0000269|PubMed:19168622, ECO:0000269|PubMed:19251861,
CC ECO:0000269|PubMed:23994560}.
CC -!- SUBUNIT: Forms a complex with cognate toxin MazF which inhibits the
CC endoribonuclease activity of MazF. {ECO:0000269|PubMed:17933891}.
CC -!- INTERACTION:
CC P0C7B4; A6QIR4: mazF; NbExp=2; IntAct=EBI-6469965, EBI-6469950;
CC -!- INDUCTION: By heat shock and by exposure to sub-MIC concentrations of
CC several antimicrobial agents such as doxycycline, erythromycin and
CC penicillin. {ECO:0000269|PubMed:17933891}.
CC -!- SIMILARITY: Belongs to the MazE/EndoAI family. {ECO:0000305}.
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DR EMBL; AP009351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_000948331.1; NZ_CP023390.1.
DR AlphaFoldDB; P0C7B4; -.
DR SMR; P0C7B4; -.
DR IntAct; P0C7B4; 1.
DR Proteomes; UP000006386; Chromosome.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.1220.10; -; 1.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
PE 1: Evidence at protein level;
KW Toxin-antitoxin system.
FT CHAIN 1..56
FT /note="Antitoxin MazE"
FT /id="PRO_0000330719"
SQ SEQUENCE 56 AA; 6252 MW; B6DA0AFB386D7691 CRC64;
MLSFSQNRSH SLEQSLKEGY SQMADLNLSL ANEAFPIECE ACDCNETYLS SNSTNE