MAZF4_MYCTU
ID MAZF4_MYCTU Reviewed; 105 AA.
AC P9WII5; L0T6U0; P64859; P71776;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Endoribonuclease MazF4 {ECO:0000305};
DE EC=3.1.-.-;
DE AltName: Full=Toxin MazF4;
DE AltName: Full=mRNA interferase MazF-mt7 {ECO:0000303|PubMed:18485066};
GN Name=mazF4; Synonyms=mazF-mt7 {ECO:0000303|PubMed:16611633};
GN OrderedLocusNames=Rv1495; ORFNames=MTCY277.17;
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, AND SUBSTRATE SPECIFICITY.
RX PubMed=18485066; DOI=10.1111/j.1365-2958.2008.06284.x;
RA Zhu L., Phadtare S., Nariya H., Ouyang M., Husson R.N., Inouye M.;
RT "The mRNA interferases, MazF-mt3 and MazF-mt7 from Mycobacterium
RT tuberculosis target unique pentad sequences in single-stranded RNA.";
RL Mol. Microbiol. 69:559-569(2008).
RN [3]
RP EXPRESSION IN 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 [4]
RP INTERACTION WITH TOPA, INHIBITION OF TOPOISOMERASE DNA CLEAVAGE, INHIBITION
RP OF MRNA CLEAVAGE BY TOPOISOMERASE, ACTIVITY REGULATION, AND EXPRESSION IN
RP M.SMEGMATIS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20724443; DOI=10.1093/nar/gkq737;
RA Huang F., He Z.G.;
RT "Characterization of an interplay between a Mycobacterium tuberculosis MazF
RT homolog, Rv1495 and its sole DNA topoisomerase I.";
RL Nucleic Acids Res. 38:8219-8230(2010).
RN [5]
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).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Acts as an endoribonuclease (mRNA interferase) on single-strand mRNA,
CC cleaving between the first and second bases in the sequence UCGCU.
CC Overexpression in M.smegmatis but not E.coli inhibits growth, this
CC effect is neutralized by coexpression with cognate toxin MazE4.
CC {ECO:0000269|PubMed:18485066}.
CC -!- FUNCTION: Residues 29-56 inhibit ssDNA cleavage by DNA topoisomerase.
CC This fragment does not have mRNA cleavage activity but it inhibits
CC growth upon overexpression in M.smegmatis.
CC {ECO:0000269|PubMed:20724443}.
CC -!- ACTIVITY REGULATION: RNA cleavage is inhibited by the C-terminal domain
CC of DNA topoisomerase I. {ECO:0000269|PubMed:20724443}.
CC -!- SUBUNIT: Forms a complex with cognate antitoxin MazE4 (By similarity).
CC Interacts with DNA topoisomerase I (PubMed:20724443).
CC {ECO:0000250|UniProtKB:P9WIH9, ECO:0000269|PubMed:20724443}.
CC -!- SIMILARITY: Belongs to the PemK/MazF family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44256.1; -; Genomic_DNA.
DR PIR; B70712; B70712.
DR RefSeq; NP_216011.1; NC_000962.3.
DR RefSeq; WP_003407593.1; NZ_NVQJ01000004.1.
DR PDB; 5XE2; X-ray; 2.01 A; A=1-105.
DR PDB; 5XE3; X-ray; 2.30 A; A/B/C/D=1-105.
DR PDBsum; 5XE2; -.
DR PDBsum; 5XE3; -.
DR AlphaFoldDB; P9WII5; -.
DR SMR; P9WII5; -.
DR STRING; 83332.Rv1495; -.
DR PaxDb; P9WII5; -.
DR DNASU; 886504; -.
DR GeneID; 45425475; -.
DR GeneID; 886504; -.
DR KEGG; mtu:Rv1495; -.
DR TubercuList; Rv1495; -.
DR eggNOG; COG2337; Bacteria.
DR OMA; GYANADN; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:2000372; P:negative regulation of DNA topoisomerase (ATP-hydrolyzing) activity; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW Toxin-antitoxin system.
FT CHAIN 1..105
FT /note="Endoribonuclease MazF4"
FT /id="PRO_0000201902"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:5XE2"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5XE2"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:5XE2"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:5XE2"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5XE2"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5XE2"
FT STRAND 62..73
FT /evidence="ECO:0007829|PDB:5XE2"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5XE2"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5XE2"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:5XE2"
SQ SEQUENCE 105 AA; 11410 MW; 52F4C417DD07EB16 CRC64;
MNAPLRGQVY RCDLGYGAKP WLIVSNNARN RHTADVVAVR LTTTRRTIPT WVAMGPSDPL
TGYVNADNIE TLGKDELGDY LGEVTPATMN KINTALATAL GLPWP
