ENDOA_BACSU
ID ENDOA_BACSU Reviewed; 116 AA.
AC P96622; Q797K4;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Endoribonuclease EndoA {ECO:0000303|PubMed:15882409};
DE EC=3.1.27.- {ECO:0000269|PubMed:15882409};
DE AltName: Full=Toxin EndoA;
DE AltName: Full=mRNA interferase EndoA;
DE AltName: Full=mRNA interferase MazF-bs {ECO:0000303|PubMed:21763692};
DE Short=MazF-bs;
GN Name=ndoA {ECO:0000303|PubMed:15882409}; Synonyms=mazF, ydcE;
GN OrderedLocusNames=BSU04660;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION AS AN ENDORIBONUCLEASE, CATALYTIC ACTIVITY, INHIBITION BY ENDOAI,
RP SUBUNIT, AND EXPRESSION IN E.COLI.
RC STRAIN=168;
RX PubMed=15882409; DOI=10.1111/j.1365-2958.2005.04606.x;
RA Pellegrini O., Mathy N., Gogos A., Shapiro L., Condon C.;
RT "The Bacillus subtilis ydcDE operon encodes an endoribonuclease of the
RT MazF/PemK family and its inhibitor.";
RL Mol. Microbiol. 56:1139-1148(2005).
RN [4]
RP FUNCTION AS AN MRNA INTERFERASE, INHIBITION BY ENDOAI, AND EXPRESSION IN
RP E.COLI.
RC STRAIN=168;
RX PubMed=21763692; DOI=10.1016/j.febslet.2011.07.008;
RA Park J.H., Yamaguchi Y., Inouye M.;
RT "Bacillus subtilis MazF-bs (EndoA) is a UACAU-specific mRNA interferase.";
RL FEBS Lett. 585:2526-2532(2011).
RN [5]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=23378533; DOI=10.1074/jbc.m112.434969;
RA Ishida Y., Park J.H., Mao L., Yamaguchi Y., Inouye M.;
RT "Replacement of all arginine residues with canavanine in MazF-bs mRNA
RT interferase changes its specificity.";
RL J. Biol. Chem. 288:7564-7571(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-116, AND SUBUNIT.
RX PubMed=14517982; DOI=10.1002/prot.10457;
RA Gogos A., Mu H., Bahna F., Gomez C.A., Shapiro L.;
RT "Crystal structure of YdcE protein from Bacillus subtilis.";
RL Proteins 53:320-322(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE OR MAZE,
RP FUNCTION, SUBUNIT, RNA-BINDING, AND MUTAGENESIS OF PHE-10; SER-19; GLN-21;
RP ARG-25; ASN-32; THR-48; GLN-50; LYS-53; LEU-56; HIS-59; ARG-71; SER-73;
RP GLU-78; GLN-79 AND ASP-90.
RC STRAIN=168;
RX PubMed=24120662; DOI=10.1016/j.molcel.2013.09.006;
RA Simanshu D.K., Yamaguchi Y., Park J.H., Inouye M., Patel D.J.;
RT "Structural basis of mRNA recognition and cleavage by toxin MazF and its
RT regulation by antitoxin MazE in Bacillus subtilis.";
RL Mol. Cell 52:447-458(2013).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Specific for 5'-UACAU-3' sequences, cleaving after the first U
CC (PubMed:21763692). Yields cleavage products with 3' phosphate and 5'
CC hydroxyl groups (PubMed:15882409). Cannot digest substrate with a
CC UUdUACAUAA cleavage site (PubMed:24120662). Overexpression is toxic for
CC cell growth (shown in E.coli), probably by inhibiting protein synthesis
CC through the cleavage of single-stranded RNA. The toxicity is reversed
CC by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE
CC from E.coli. The EndoA-EndoAI complex does not seem to bind its own
CC promoter (PubMed:24120662). {ECO:0000269|PubMed:15882409,
CC ECO:0000269|PubMed:21763692, ECO:0000269|PubMed:23378533,
CC ECO:0000269|PubMed:24120662}.
CC -!- SUBUNIT: Homodimer (PubMed:14517982, PubMed:24120662). Forms a complex
CC with antitoxin EndoAI in which the toxin activity is inhibited
CC (PubMed:15882409). One dimer binds a ssRNA substrate, forms a
CC heterohexamer composed of alternating toxin and antitoxin homodimers
CC which inhibits the endoribonuclease activity. Antitoxin prevents RNA
CC binding to the endoribonuclease (PubMed:24120662).
CC {ECO:0000269|PubMed:14517982, ECO:0000269|PubMed:15882409,
CC ECO:0000269|PubMed:24120662}.
CC -!- MISCELLANEOUS: Replacing all Arg residues by canavanine yields an
CC enzyme that recognizes a longer consensus sequence UACAUA, thus
CC altering its substrate specificity. Still cleaves between the first and
CC second nucleotides. {ECO:0000269|PubMed:23378533}.
CC -!- SIMILARITY: Belongs to the PemK/MazF family. {ECO:0000305}.
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DR EMBL; AB001488; BAA19303.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12273.1; -; Genomic_DNA.
DR PIR; C69773; C69773.
DR RefSeq; NP_388347.1; NC_000964.3.
DR RefSeq; WP_003156187.1; NZ_JNCM01000031.1.
DR PDB; 1NE8; X-ray; 2.10 A; A=2-116.
DR PDB; 4MDX; X-ray; 1.50 A; A/B=1-116.
DR PDB; 4ME7; X-ray; 2.92 A; A/B/C/D=2-116.
DR PDBsum; 1NE8; -.
DR PDBsum; 4MDX; -.
DR PDBsum; 4ME7; -.
DR AlphaFoldDB; P96622; -.
DR SMR; P96622; -.
DR STRING; 224308.BSU04660; -.
DR DrugBank; DB02042; 2-(2-{2-[2-(2-Methoxy-Ethoxy)-Ethoxy]-Ethoxy}-Ethoxy)-Ethanol.
DR jPOST; P96622; -.
DR PaxDb; P96622; -.
DR PRIDE; P96622; -.
DR EnsemblBacteria; CAB12273; CAB12273; BSU_04660.
DR GeneID; 64302332; -.
DR GeneID; 66327524; -.
DR GeneID; 939935; -.
DR KEGG; bsu:BSU04660; -.
DR PATRIC; fig|224308.179.peg.494; -.
DR eggNOG; COG2337; Bacteria.
DR InParanoid; P96622; -.
DR OMA; NDIGNQY; -.
DR PhylomeDB; P96622; -.
DR BioCyc; BSUB:BSU04660-MON; -.
DR EvolutionaryTrace; P96622; -.
DR PRO; PR:P96622; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
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 RNA-binding; Toxin-antitoxin system.
FT CHAIN 1..116
FT /note="Endoribonuclease EndoA"
FT /id="PRO_0000201900"
FT SITE 25
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:24120662"
FT MUTAGEN 10
FT /note="F->A: Remains toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 19
FT /note="S->A: Partially toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 21
FT /note="Q->A: Not toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 25
FT /note="R->A: Not toxic in E.coli, 50-fold decreased RNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 32
FT /note="N->A: Not toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 48
FT /note="T->A: Not toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 50
FT /note="Q->A: Remains toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 53
FT /note="K->A: Not toxic in E.coli, 70-fold decreased RNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 56
FT /note="L->A: Not toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 59
FT /note="H->A: Not toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 71
FT /note="R->A: Remains toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 73
FT /note="S->A: Not toxic in E.coli, 100-fold decreased RNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 78
FT /note="E->A: Not toxic in E.coli, 625-fold decreased RNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 79
FT /note="Q->A: Not toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 90
FT /note="D->A: Remains toxic in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:4MDX"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4MDX"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:4MDX"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:4MDX"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4MDX"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4MDX"
FT STRAND 73..84
FT /evidence="ECO:0007829|PDB:4MDX"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4MDX"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:4MDX"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:4MDX"
SQ SEQUENCE 116 AA; 12978 MW; FE89144E62BD2B7C CRC64;
MIVKRGDVYF ADLSPVVGSE QGGVRPVLVI QNDIGNRFSP TAIVAAITAQ IQKAKLPTHV
EIDAKRYGFE RDSVILLEQI RTIDKQRLTD KITHLDDEMM DKVDEALQIS LALIDF
