ID   MAZF_STAHJ              Reviewed;         121 AA.
AC   Q4L7V3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Endoribonuclease MazF;
DE            EC=3.1.-.-;
DE   AltName: Full=Toxin MazF;
DE   AltName: Full=mRNA interferase MazF;
GN   Name=mazF; OrderedLocusNames=SH0963;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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CC   -!- SUBUNIT: Forms a complex with MazE which is no longer active as an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; AP006716; BAE04272.1; -; Genomic_DNA.
DR   RefSeq; WP_011275272.1; NC_007168.1.
DR   AlphaFoldDB; Q4L7V3; -.
DR   SMR; Q4L7V3; -.
DR   STRING; 279808.SH0963; -.
DR   EnsemblBacteria; BAE04272; BAE04272; SH0963.
DR   GeneID; 58062855; -.
DR   KEGG; sha:SH0963; -.
DR   eggNOG; COG2337; Bacteria.
DR   HOGENOM; CLU_121823_1_0_9; -.
DR   OMA; NDIGNQY; -.
DR   OrthoDB; 1754531at2; -.
DR   Proteomes; UP000000543; 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   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; RNA-binding; Toxin-antitoxin system.
FT   CHAIN           1..121
FT                   /note="Endoribonuclease MazF"
FT                   /id="PRO_0000330708"
SQ   SEQUENCE   121 AA;  13673 MW;  B50A7EC621B4656C CRC64;
     MIRRGDVYLA DLSPVQGSEQ GGVRPVVIIQ NDTGNKYSPT VIVAAITGRI NKAKIPTHVE
     IEKKKYRLDK DSVILLEQIR TLDKKRLKEK LTYLSDEKMQ EVDEALDISL GLHDEVKTQN
     T