SP0E_BACSU
ID SP0E_BACSU Reviewed; 85 AA.
AC P05043;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Aspartyl-phosphate phosphatase Spo0E;
DE EC=3.1.3.-;
DE AltName: Full=Stage 0 sporulation protein E;
DE AltName: Full=Stage 0 sporulation regulatory protein Spo0E;
GN Name=spo0E; OrderedLocusNames=BSU13640;
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;
RX PubMed=2838724; DOI=10.1111/j.1365-2958.1987.tb00536.x;
RA Perego M., Hoch J.A.;
RT "Isolation and sequence of the spo0E gene: its role in initiation of
RT sporulation in Bacillus subtilis.";
RL Mol. Microbiol. 1:125-132(1987).
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 PROTEIN SEQUENCE OF 1-7, FUNCTION, AND MUTAGENESIS OF THE C-TERMINUS.
RX PubMed=8127878; DOI=10.1073/pnas.91.5.1756;
RA Ohlsen K.L., Grimsley J.K., Hoch J.A.;
RT "Deactivation of the sporulation transcription factor Spo0A by the Spo0E
RT protein phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1756-1760(1994).
RN [4]
RP FUNCTION.
RX PubMed=11112444; DOI=10.1006/bbrc.2000.3911;
RA Nanamiya H., Takahashi K., Fujita M., Kawamura F.;
RT "Deficiency of the initiation events of sporulation in Bacillus subtilis
RT clpP mutant can be suppressed by a lack of the Spo0E protein phosphatase.";
RL Biochem. Biophys. Res. Commun. 279:229-233(2000).
RN [5]
RP FUNCTION, AND INTERACTION WITH SPO0A.
RX PubMed=12067336; DOI=10.1046/j.1365-2958.2002.02974.x;
RA Stephenson S.J., Perego M.;
RT "Interaction surface of the Spo0A response regulator with the Spo0E
RT phosphatase.";
RL Mol. Microbiol. 44:1455-1467(2002).
RN [6]
RP FUNCTION.
RX PubMed=15057450; DOI=10.1007/s00284-003-4186-2;
RA Shafikhani S.H., Leighton T.;
RT "AbrB and Spo0E control the proper timing of sporulation in Bacillus
RT subtilis.";
RL Curr. Microbiol. 48:262-269(2004).
RN [7]
RP FUNCTION, INTERACTION WITH SPO0A, AND MUTAGENESIS OF ILE-36; SER-39;
RP GLN-40; LEU-42; ASP-43; LEU-45 AND ILE-46.
RX PubMed=18045868; DOI=10.1074/jbc.m709032200;
RA Diaz A.R., Stephenson S., Green J.M., Levdikov V.M., Wilkinson A.J.,
RA Perego M.;
RT "Functional role for a conserved aspartate in the Spo0E signature motif
RT involved in the dephosphorylation of the Bacillus subtilis sporulation
RT regulator Spo0A.";
RL J. Biol. Chem. 283:2962-2972(2008).
RN [8]
RP DEGRADATION BY FTSH.
RC STRAIN=1012;
RX PubMed=19332814; DOI=10.1099/mic.0.024182-0;
RA Le A.T., Schumann W.;
RT "The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH
RT metalloprotease.";
RL Microbiology 155:1122-1132(2009).
CC -!- FUNCTION: Aspartyl-phosphate phosphatase which specifically
CC dephosphorylates the sporulation transcription factor Spo0A-P and
CC negatively regulates the sporulation initiation pathway in order to
CC control the proper timing of sporulation. {ECO:0000269|PubMed:11112444,
CC ECO:0000269|PubMed:12067336, ECO:0000269|PubMed:15057450,
CC ECO:0000269|PubMed:18045868, ECO:0000269|PubMed:8127878}.
CC -!- SUBUNIT: Interacts with Spo0A. {ECO:0000269|PubMed:12067336,
CC ECO:0000269|PubMed:18045868}.
CC -!- PTM: Probably degraded by FtsH, the last 14 residues seem to form the
CC FtsH recognition site.
CC -!- MISCELLANEOUS: Mutations that block the onset of sporulation in
CC Bacillus subtilis are called stage 0 mutations, or spo0 mutations, and
CC at least eight genetic loci have been identified in which a mutation
CC can result in a stage 0 phenotype. Stage 0 mutants lack the ability to
CC form the asymmetric septum characteristic of the initiation of the
CC sporulation process. In addition, these mutations have many pleiotropic
CC effects on the synthesis of a variety of transcripts by minor forms of
CC RNA polymerase in this organism.
CC -!- SIMILARITY: Belongs to the spo0E family. {ECO:0000305}.
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DR EMBL; Y00526; CAA68583.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13237.1; -; Genomic_DNA.
DR PIR; S03746; S03746.
DR RefSeq; NP_389247.1; NC_000964.3.
DR RefSeq; WP_003218598.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P05043; -.
DR SMR; P05043; -.
DR STRING; 224308.BSU13640; -.
DR PaxDb; P05043; -.
DR PRIDE; P05043; -.
DR EnsemblBacteria; CAB13237; CAB13237; BSU_13640.
DR GeneID; 64303254; -.
DR GeneID; 939315; -.
DR KEGG; bsu:BSU13640; -.
DR PATRIC; fig|224308.179.peg.1481; -.
DR OMA; MMIDAAN; -.
DR BioCyc; BSUB:BSU13640-MON; -.
DR PRO; PR:P05043; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0043937; P:regulation of sporulation; IGI:CACAO.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR018540; Spo0E-like.
DR InterPro; IPR037208; Spo0E-like_sf.
DR Pfam; PF09388; SpoOE-like; 1.
DR SUPFAM; SSF140500; SSF140500; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Reference proteome; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..85
FT /note="Aspartyl-phosphate phosphatase Spo0E"
FT /id="PRO_0000072053"
FT MUTAGEN 36
FT /note="I->A: Impairs sporulation inhibition activity."
FT /evidence="ECO:0000269|PubMed:18045868"
FT MUTAGEN 39
FT /note="S->A: Impairs sporulation inhibition activity."
FT /evidence="ECO:0000269|PubMed:18045868"
FT MUTAGEN 40
FT /note="Q->A: Impairs sporulation inhibition activity."
FT /evidence="ECO:0000269|PubMed:18045868"
FT MUTAGEN 42
FT /note="L->A: Impairs sporulation inhibition activity."
FT /evidence="ECO:0000269|PubMed:18045868"
FT MUTAGEN 43
FT /note="D->A: Impairs sporulation inhibition activity."
FT /evidence="ECO:0000269|PubMed:18045868"
FT MUTAGEN 45
FT /note="L->A: Impairs sporulation inhibition activity."
FT /evidence="ECO:0000269|PubMed:18045868"
FT MUTAGEN 46
FT /note="I->A: Impairs sporulation inhibition activity."
FT /evidence="ECO:0000269|PubMed:18045868"
FT MUTAGEN 71..85
FT /note="Missing: In spo0E11; a hyperactive phosphatase, it
FT is no longer a substrate for FtsH."
FT /evidence="ECO:0000269|PubMed:8127878"
SQ SEQUENCE 85 AA; 9791 MW; 4FDF18420E77B9CF CRC64;
MGGSSEQERL LVSIDEKRKL MIDAARKQGF TGHDTIRHSQ ELDCLINEYH QLMQENEHSQ
GIQGLVKKLG LWPRRDVMPA YDANK
