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   27-MAR-2024, entry version 134.
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; Bacillota; 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; 224308-BSU04660; -.
DR   EnsemblBacteria; CAB12273; CAB12273; BSU_04660.
DR   GeneID; 83883721; -.
DR   GeneID; 939935; -.
DR   KEGG; bsu:BSU04660; -.
DR   PATRIC; fig|224308.179.peg.494; -.
DR   eggNOG; COG2337; Bacteria.
DR   InParanoid; P96622; -.
DR   OrthoDB; 9808744at2; -.
DR   PhylomeDB; P96622; -.
DR   BioCyc; BSUB:BSU04660-MONOMER; -.
DR   EvolutionaryTrace; P96622; -.
DR   PRO; PR:P96622; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:RNA endonuclease activity; IBA:GO_Central.
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:SF2; ENDORIBONUCLEASE MAZF; 1.
DR   PANTHER; PTHR33988; ENDORIBONUCLEASE MAZF-RELATED; 1.
DR   Pfam; PF02452; PemK_toxin; 1.
DR   PIRSF; PIRSF033490; MazF; 1.
DR   SUPFAM; SSF50118; Cell growth inhibitor/plasmid maintenance toxic component; 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
FT                   RNA-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
FT                   RNA-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
FT                   RNA-binding."
FT                   /evidence="ECO:0000269|PubMed:24120662"
FT   MUTAGEN         78
FT                   /note="E->A: Not toxic in E.coli, 625-fold decreased
FT                   RNA-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
//