MAZF_STAAM
ID MAZF_STAAM Reviewed; 120 AA.
AC Q7A2N3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Endoribonuclease MazF;
DE EC=3.1.-.-;
DE AltName: Full=Toxin MazF;
DE AltName: Full=mRNA interferase MazF;
GN Name=mazF; OrderedLocusNames=SAV2068;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), AND SUBUNIT.
RA Park J.Y., Im H., Seok S.H., Lee B.J.;
RT "Structural insights into the toxin from Staphylococcus aureus Mu50.";
RL Submitted (JAN-2015) to the PDB data bank.
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: Homodimer (Ref.2). Forms a complex with MazE which is no
CC longer active as an endoribonuclease. {ECO:0000250|UniProtKB:A6QIR4,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the PemK/MazF family. {ECO:0000305}.
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DR EMBL; BA000017; BAB58230.1; -; Genomic_DNA.
DR RefSeq; WP_000621175.1; NC_002758.2.
DR PDB; 4OF1; X-ray; 2.45 A; A/B=1-120.
DR PDBsum; 4OF1; -.
DR AlphaFoldDB; Q7A2N3; -.
DR SMR; Q7A2N3; -.
DR PaxDb; Q7A2N3; -.
DR EnsemblBacteria; BAB58230; BAB58230; SAV2068.
DR KEGG; sav:SAV2068; -.
DR HOGENOM; CLU_121823_1_0_9; -.
DR OMA; NDIGNQY; -.
DR PhylomeDB; Q7A2N3; -.
DR BioCyc; SAUR158878:SAV_RS11320-MON; -.
DR Proteomes; UP000002481; 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 3D-structure; Endonuclease; Hydrolase; Nuclease; RNA-binding;
KW Toxin-antitoxin system.
FT CHAIN 1..120
FT /note="Endoribonuclease MazF"
FT /id="PRO_0000330699"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:4OF1"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:4OF1"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:4OF1"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:4OF1"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4OF1"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4OF1"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:4OF1"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4OF1"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4OF1"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:4OF1"
SQ SEQUENCE 120 AA; 13442 MW; 41D531536BAE2B57 CRC64;
MIRRGDVYLA DLSPVQGSEQ GGVRPVVIIQ NDTGNKYSPT VIVAAITGRI NKAKIPTHVE
IEKKKYKLDK DSVILLEQIR TLDKKRLKEK LTYLSDDKMK EVDNALMISL GLNAVAHQKN