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MAZF_STAAN
ID   MAZF_STAAN              Reviewed;         120 AA.
AC   Q7A4G9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Endoribonuclease MazF;
DE            EC=3.1.-.-;
DE   AltName: Full=SaMazF {ECO:0000303|PubMed:21213075};
DE   AltName: Full=Toxin MazF;
DE   AltName: Full=mRNA interferase MazF;
GN   Name=mazF; OrderedLocusNames=SA1873;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
RN   [3]
RP   STRUCTURE BY NMR OF 2-120, AND SUBUNIT.
RX   PubMed=21213075; DOI=10.1007/s12104-010-9290-1;
RA   Zorzini V., Haesaerts S., Cheung A., Loris R., van Nuland N.A.;
RT   "1H, 13C, and 15N backbone and side-chain chemical shift assignment of the
RT   staphylococcal MazF mRNA interferase.";
RL   Biomol. NMR. Assign. 5:157-160(2011).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-120, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=24748664; DOI=10.1093/nar/gku266;
RA   Zorzini V., Buts L., Sleutel M., Garcia-Pino A., Talavera A., Haesaerts S.,
RA   De Greve H., Cheung A., van Nuland N.A., Loris R.;
RT   "Structural and biophysical characterization of Staphylococcus aureus
RT   SaMazF shows conservation of functional dynamics.";
RL   Nucleic Acids Res. 42:6709-6725(2014).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system,
CC       cannot be expressed in E.coli in the absence of cognate antitoxin MazE
CC       (PubMed:24748664). Ribosome-independent, sequence-specific
CC       endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis
CC       and inducing bacterial stasis; it cuts between the first and
CC       nucleotides of 5'-UACAU-3' in single-stranded RNA (By similarity). Its
CC       endoribnuclease activity is neutralized by coexpression with cognate
CC       antitoxin MazE (PubMed:24748664). {ECO:0000250|UniProtKB:A6QIR4,
CC       ECO:0000269|PubMed:24748664}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable at 90 degrees Celsius. {ECO:0000269|PubMed:24748664};
CC   -!- SUBUNIT: Homodimer. Forms a complex with MazE which inhibits the
CC       endoribonuclease activity of MazF. {ECO:0000269|PubMed:24748664,
CC       ECO:0000305|PubMed:21213075}.
CC   -!- SIMILARITY: Belongs to the PemK/MazF family. {ECO:0000305}.
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DR   EMBL; BA000018; BAB43155.1; -; Genomic_DNA.
DR   PIR; B89999; B89999.
DR   RefSeq; WP_000621175.1; NC_002745.2.
DR   PDB; 2MF2; NMR; -; A/B=2-120.
DR   PDB; 4MZM; X-ray; 2.10 A; A/B/C/D=2-120.
DR   PDB; 4MZP; X-ray; 2.70 A; A/B/C/D/E/F/G/H=2-120.
DR   PDB; 4MZT; X-ray; 2.30 A; A/B=2-120.
DR   PDBsum; 2MF2; -.
DR   PDBsum; 4MZM; -.
DR   PDBsum; 4MZP; -.
DR   PDBsum; 4MZT; -.
DR   AlphaFoldDB; Q7A4G9; -.
DR   SMR; Q7A4G9; -.
DR   EnsemblBacteria; BAB43155; BAB43155; BAB43155.
DR   KEGG; sau:SA1873; -.
DR   HOGENOM; CLU_121823_1_0_9; -.
DR   OMA; NDIGNQY; -.
DR   Proteomes; UP000000751; 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_0000330701"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   STRAND          22..28
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   HELIX           32..37
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   STRAND          39..48
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   TURN            63..67
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   STRAND          72..83
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:4MZM"
FT   HELIX           96..109
FT                   /evidence="ECO:0007829|PDB:4MZM"
SQ   SEQUENCE   120 AA;  13442 MW;  41D531536BAE2B57 CRC64;
     MIRRGDVYLA DLSPVQGSEQ GGVRPVVIIQ NDTGNKYSPT VIVAAITGRI NKAKIPTHVE
     IEKKKYKLDK DSVILLEQIR TLDKKRLKEK LTYLSDDKMK EVDNALMISL GLNAVAHQKN
 
 
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