MAZF_STAAS
ID MAZF_STAAS Reviewed; 120 AA.
AC Q6G7P1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Endoribonuclease MazF;
DE EC=3.1.-.-;
DE AltName: Full=Toxin MazF;
DE AltName: Full=mRNA interferase MazF;
GN Name=mazF; OrderedLocusNames=SAS1973;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Ribosome-independent, sequence-specific endoribonuclease that cleaves
CC mRNA, thus inhibiting protein synthesis and inducing bacterial stasis.
CC It cuts between the first and nucleotides of 5'-UACAU-3' in single-
CC stranded RNA. Neutralized by coexpression with cognate antitoxin MazE.
CC {ECO:0000250|UniProtKB:A6QIR4}.
CC -!- SUBUNIT: Forms a complex with MazE which is no longer active as an
CC endoribonuclease. {ECO:0000250|UniProtKB:A6QIR4}.
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; BX571857; CAG43780.1; -; Genomic_DNA.
DR RefSeq; WP_000621175.1; NC_002953.3.
DR AlphaFoldDB; Q6G7P1; -.
DR SMR; Q6G7P1; -.
DR KEGG; sas:SAS1973; -.
DR HOGENOM; CLU_121823_1_0_9; -.
DR OMA; NDIGNQY; -.
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 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; RNA-binding; Toxin-antitoxin system.
FT CHAIN 1..120
FT /note="Endoribonuclease MazF"
FT /id="PRO_0000330697"
SQ SEQUENCE 120 AA; 13442 MW; 41D531536BAE2B57 CRC64;
MIRRGDVYLA DLSPVQGSEQ GGVRPVVIIQ NDTGNKYSPT VIVAAITGRI NKAKIPTHVE
IEKKKYKLDK DSVILLEQIR TLDKKRLKEK LTYLSDDKMK EVDNALMISL GLNAVAHQKN