MAZF9_MYCTU
ID MAZF9_MYCTU Reviewed; 118 AA.
AC P71650; L0TAP2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Endoribonuclease MazF9 {ECO:0000305};
DE EC=3.1.-.-;
DE AltName: Full=Toxin MazF9 {ECO:0000303|PubMed:16611633};
DE AltName: Full=mRNA interferase MazF-mt1 {ECO:0000303|PubMed:16611633};
GN Name=mazF9; Synonyms=mazF-mt1 {ECO:0000303|PubMed:16611633};
GN OrderedLocusNames=Rv2801c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS AN MRNA INTERFERASE, SUBSTRATE SPECIFICITY, AND EXPRESSION IN
RP E.COLI.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16611633; DOI=10.1074/jbc.m512693200;
RA Zhu L., Zhang Y., Teh J.S., Zhang J., Connell N., Rubin H., Inouye M.;
RT "Characterization of mRNA interferases from Mycobacterium tuberculosis.";
RL J. Biol. Chem. 281:18638-18643(2006).
RN [3]
RP EXPRESSION IN E.COLI, AND FUNCTION AS A TOXIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19016878; DOI=10.1111/j.1574-6968.2008.01400.x;
RA Gupta A.;
RT "Killing activity and rescue function of genome-wide toxin-antitoxin loci
RT of Mycobacterium tuberculosis.";
RL FEMS Microbiol. Lett. 290:45-53(2009).
RN [4]
RP EXPRESSION IN M.SMEGMATIS, AND FUNCTION AS A TOXIN.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=20011113; DOI=10.1371/journal.pgen.1000767;
RA Ramage H.R., Connolly L.E., Cox J.S.;
RT "Comprehensive functional analysis of Mycobacterium tuberculosis toxin-
RT antitoxin systems: implications for pathogenesis, stress responses, and
RT evolution.";
RL PLoS Genet. 5:E1000767-E1000767(2009).
RN [5]
RP FUNCTION AS A TOXIN, AND INTERACTION WITH ANTITOXINS MAZE9; VAPB27 AND
RP VAPB40.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20876537; DOI=10.1074/jbc.m110.163105;
RA Zhu L., Sharp J.D., Kobayashi H., Woychik N.A., Inouye M.;
RT "Noncognate Mycobacterium tuberculosis toxin-antitoxins can physically and
RT functionally interact.";
RL J. Biol. Chem. 285:39732-39738(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [7]
RP FUNCTION, INTERACTION WITH MAZE9, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=25608501; DOI=10.1038/ncomms7059;
RA Tiwari P., Arora G., Singh M., Kidwai S., Narayan O.P., Singh R.;
RT "MazF ribonucleases promote Mycobacterium tuberculosis drug tolerance and
RT virulence in guinea pigs.";
RL Nat. Commun. 6:6059-6059(2015).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Upon expression in E.coli and M.smegmatis inhibits cell growth and
CC colony formation. Its toxic effect is neutralized by coexpression with
CC cognate antitoxin MazE9. Acts as an mRNA interferase, specifically
CC cleaving between U and C in UAC sequences. May cleave its cognate
CC antitoxin's gene (PubMed:25608501). In E.coli expression with non-
CC cognate antitoxins VapB27 and VapB40 partially neutralizes the toxin.
CC {ECO:0000269|PubMed:16611633, ECO:0000269|PubMed:19016878,
CC ECO:0000269|PubMed:20011113, ECO:0000269|PubMed:20876537,
CC ECO:0000269|PubMed:25608501}.
CC -!- SUBUNIT: Forms a complex with cognate antitoxin MazE9.
CC {ECO:0000269|PubMed:20876537, ECO:0000269|PubMed:25608501}.
CC -!- INDUCTION: Mildy induced (5 to 9-fold) by oxidative and nitrosative
CC stress, starvation, growth in the presence of isoniazid or gentamycin,
CC strongly induced (24-fold) when grown in a non-replicating state.
CC {ECO:0000269|PubMed:25608501}.
CC -!- DISRUPTION PHENOTYPE: Individual deletion of mazF3, mazF6 and mazF9
CC have little to no phenotype, but a triple mutant shows increased
CC sensitivity to oxidative and antibiotic stress and starvation,
CC decreased formation of persisters cells, and a decreased bacterial load
CC and pathogenic damage in infected guinea pigs.
CC {ECO:0000269|PubMed:25608501}.
CC -!- SIMILARITY: Belongs to the PemK/MazF family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45600.1; -; Genomic_DNA.
DR PIR; D70689; D70689.
DR RefSeq; NP_217317.1; NC_000962.3.
DR RefSeq; WP_003414166.1; NZ_NVQJ01000020.1.
DR PDB; 5HJZ; X-ray; 1.98 A; A/B=1-118.
DR PDB; 6KYS; X-ray; 2.20 A; A/B=2-118.
DR PDB; 6KYT; X-ray; 2.00 A; A/B/D/E/G/H/J/K=1-118.
DR PDB; 6L29; X-ray; 2.30 A; A/B=2-118.
DR PDB; 6L2A; X-ray; 1.90 A; A=2-118.
DR PDB; 7DU5; X-ray; 2.65 A; A/B=2-118.
DR PDBsum; 5HJZ; -.
DR PDBsum; 6KYS; -.
DR PDBsum; 6KYT; -.
DR PDBsum; 6L29; -.
DR PDBsum; 6L2A; -.
DR PDBsum; 7DU5; -.
DR AlphaFoldDB; P71650; -.
DR SMR; P71650; -.
DR STRING; 83332.Rv2801c; -.
DR PaxDb; P71650; -.
DR DNASU; 888921; -.
DR GeneID; 888921; -.
DR KEGG; mtu:Rv2801c; -.
DR TubercuList; Rv2801c; -.
DR eggNOG; COG2337; Bacteria.
DR InParanoid; P71650; -.
DR OMA; NDIGNQY; -.
DR PhylomeDB; P71650; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:MTBBASE.
DR GO; GO:0044003; P:modulation by symbiont of host process; IMP:MTBBASE.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:MTBBASE.
DR GO; GO:0045926; P:negative regulation of growth; IDA:MTBBASE.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
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; Reference proteome;
KW Toxin-antitoxin system.
FT CHAIN 1..118
FT /note="Endoribonuclease MazF9"
FT /id="PRO_0000406309"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:6L2A"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:6L2A"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:6L2A"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:6L2A"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6L2A"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6L2A"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6KYT"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6L2A"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6L2A"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6L2A"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6L2A"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6L2A"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:6L2A"
SQ SEQUENCE 118 AA; 12891 MW; 9D378205050CE46F CRC64;
MMRRGEIWQV DLDPARGSEA NNQRPAVVVS NDRANATATR LGRGVITVVP VTSNIAKVYP
FQVLLSATTT GLQVDCKAQA EQIRSIATER LLRPIGRVSA AELAQLDEAL KLHLDLWS
