ENDAI_BACSU
ID ENDAI_BACSU Reviewed; 93 AA.
AC P96621; Q797K5;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Antitoxin EndoAI {ECO:0000303|PubMed:15882409};
DE AltName: Full=Antitoxin MazE-bs;
DE Short=MazE-bs;
DE AltName: Full=EndoA inhibitor;
GN Name=ndoAI {ECO:0000303|PubMed:15882409}; Synonyms=mazE;
GN OrderedLocusNames=BSU04650;
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 ANTITOXIN, 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 ANTITOXIN, AND EXPRESSION IN 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 X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 2-93 IN COMPLEX WITH MAZF,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF TYR-61; MET-64; ASN-68; SER-72;
RP GLU-74 AND GLU-79.
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: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Antitoxin that directly inhibits activity of EndoA in vitro. Upon
CC expression in E.coli counteracts inhibitory effect of endoribonuclease
CC EndoA. The EndoA-EndoAI complex does not seem to bind its own promoter
CC (PubMed:24120662). {ECO:0000269|PubMed:15882409,
CC ECO:0000269|PubMed:21763692, ECO:0000269|PubMed:24120662}.
CC -!- SUBUNIT: Homodimer, forms a heterohexamer composed of alternating toxin
CC and antitoxin homodimers which inhibits the toxin's endoribonuclease
CC activity. Antitoxin prevents RNA binding to the endoribonuclease
CC (PubMed:24120662). {ECO:0000269|PubMed:15882409,
CC ECO:0000269|PubMed:24120662}.
CC -!- INTERACTION:
CC P96621; P96621: ndoAI; NbExp=2; IntAct=EBI-7370294, EBI-7370294;
CC -!- SIMILARITY: Belongs to the MazE/EndoAI family. {ECO:0000305}.
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DR EMBL; AB001488; BAA19302.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12272.1; -; Genomic_DNA.
DR PIR; B69773; B69773.
DR RefSeq; NP_388346.1; NC_000964.3.
DR RefSeq; WP_003225183.1; NZ_JNCM01000031.1.
DR PDB; 4ME7; X-ray; 2.92 A; E/F=2-93.
DR PDBsum; 4ME7; -.
DR AlphaFoldDB; P96621; -.
DR SMR; P96621; -.
DR MINT; P96621; -.
DR STRING; 224308.BSU04650; -.
DR PaxDb; P96621; -.
DR PRIDE; P96621; -.
DR EnsemblBacteria; CAB12272; CAB12272; BSU_04650.
DR GeneID; 50134768; -.
DR GeneID; 64302331; -.
DR GeneID; 938177; -.
DR KEGG; bsu:BSU04650; -.
DR PATRIC; fig|224308.179.peg.493; -.
DR eggNOG; COG0864; Bacteria.
DR OMA; ENECFAG; -.
DR PhylomeDB; P96621; -.
DR BioCyc; BSUB:BSU04650-MON; -.
DR PRO; PR:P96621; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.1220.10; -; 1.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR002145; CopG.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR Pfam; PF01402; RHH_1; 1.
DR SUPFAM; SSF47598; SSF47598; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..93
FT /note="Antitoxin EndoAI"
FT /id="PRO_0000086974"
FT MUTAGEN 61
FT /note="Y->A: No longer prevents EndoA toxicity upon
FT coexpression in E.coli, due to loss of EndoA-EndoAI
FT interaction."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 64
FT /note="M->A: Still prevents EndoA toxicity upon
FT coexpression in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 68
FT /note="N->A: Still prevents EndoA toxicity upon
FT coexpression in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 72
FT /note="S->A: Still prevents EndoA toxicity upon
FT coexpression in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 74
FT /note="E->A: Still prevents EndoA toxicity upon
FT coexpression in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT MUTAGEN 79
FT /note="E->A: Still prevents EndoA toxicity upon
FT coexpression in E.coli."
FT /evidence="ECO:0000269|PubMed:24120662"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:4ME7"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:4ME7"
FT HELIX 33..74
FT /evidence="ECO:0007829|PDB:4ME7"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4ME7"
SQ SEQUENCE 93 AA; 10547 MW; FA77E052B42BC28D CRC64;
MSESSARTEM KISLPENLVA ELDGVAMREK RSRNELISQA VRAYVSERTT RHNRDLMRRG
YMEMAKINLN ISSEAHFAEC EAETTVERLV SGG
