MAZF_STAAE
ID MAZF_STAAE Reviewed; 120 AA.
AC A6QIR4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Endoribonuclease MazF;
DE EC=3.1.-.-;
DE AltName: Full=MazFSa {ECO:0000303|PubMed:17933891};
DE AltName: Full=Toxin MazF;
DE AltName: Full=mRNA interferase MazF;
GN Name=mazF; OrderedLocusNames=NWMN_1974;
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 ENDORIBONUCLEASE, 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, AND SUBSTRATE SPECIFICITY.
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: Toxic component of a type II toxin-antitoxin (TA) system. A
CC sequence-specific endoribonuclease, it cuts between the first and
CC second nucleotides of 5'-UACAU-3' (PubMed:19251861, PubMed:23994560).
CC Cleaves the artificial ssDNA-RNA substrate 5'-AAGTCrUrACATCAG-3'
CC between rU and rA in vitro (PubMed:23994560). Originally found to be a
CC ribosome-independent, with a consensus sequence of 5'-[ACG]UU[ACG]-3'
CC in single-stranded RNA (PubMed:17933891, PubMed:19168622). Its
CC overexpression inhibits protein synthesis and induces bacterial stasis,
CC it is neutralized by coexpression with cognate antitoxin MazE
CC (PubMed:17933891, PubMed:19168622, PubMed:19251861). Not all mRNAs are
CC equally susceptible in vivo (gyrB, recA and sarA for example are not
CC degraded), while no degradation of rRNA has been seen
CC (PubMed:19168622). {ECO:0000269|PubMed:17933891,
CC ECO:0000269|PubMed:19168622, ECO:0000269|PubMed:19251861,
CC ECO:0000269|PubMed:23994560}.
CC -!- SUBUNIT: Forms a complex with MazE which is no longer active as an
CC endoribonuclease. {ECO:0000269|PubMed:17933891}.
CC -!- INTERACTION:
CC A6QIR4; P0C7B4: mazE; NbExp=2; IntAct=EBI-6469950, EBI-6469965;
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 -!- MISCELLANEOUS: The cleavage efficiency was significantly reduced if the
CC first or fourth residues of the consensus region were changed to U.
CC Alterations in any of the two U residues in the center of the consensus
CC sequence completely abolished the cleavage by MazF.
CC {ECO:0000269|PubMed:17933891}.
CC -!- SIMILARITY: Belongs to the PemK/MazF 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; AP009351; BAF68246.1; -; Genomic_DNA.
DR RefSeq; WP_000621175.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QIR4; -.
DR BMRB; A6QIR4; -.
DR SMR; A6QIR4; -.
DR IntAct; A6QIR4; 1.
DR EnsemblBacteria; BAF68246; BAF68246; NWMN_1974.
DR KEGG; sae:NWMN_1974; -.
DR HOGENOM; CLU_121823_1_0_9; -.
DR OMA; NDIGNQY; -.
DR Proteomes; UP000006386; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.110; -; 1.
DR InterPro; IPR003477; PemK-like.
DR InterPro; IPR011067; Plasmid_toxin/cell-grow_inhib.
DR PANTHER; PTHR33988; PTHR33988; 1.
DR Pfam; PF02452; PemK_toxin; 1.
DR PIRSF; PIRSF033490; MazF; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Nuclease; RNA-binding; Toxin-antitoxin system.
FT CHAIN 1..120
FT /note="Endoribonuclease MazF"
FT /id="PRO_0000330703"
SQ SEQUENCE 120 AA; 13442 MW; 41D531536BAE2B57 CRC64;
MIRRGDVYLA DLSPVQGSEQ GGVRPVVIIQ NDTGNKYSPT VIVAAITGRI NKAKIPTHVE
IEKKKYKLDK DSVILLEQIR TLDKKRLKEK LTYLSDDKMK EVDNALMISL GLNAVAHQKN
