ID   YNZD_BACSU              Reviewed;          57 AA.
AC   O31819;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Aspartyl-phosphate phosphatase YnzD;
DE            EC=3.1.3.-;
DE   AltName: Full=Stage 0 sporulation regulatory protein YnzD;
GN   Name=ynzD; OrderedLocusNames=BSU17920;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=11679073; DOI=10.1046/j.1365-2958.2001.02611.x;
RA   Perego M.;
RT   "A new family of aspartyl phosphate phosphatases targeting the sporulation
RT   transcription factor Spo0A of Bacillus subtilis.";
RL   Mol. Microbiol. 42:133-143(2001).
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.
CC       {ECO:0000269|PubMed:11679073}.
CC   -!- INDUCTION: During exponential phase and in conditions antithetical to
CC       sporulation. {ECO:0000269|PubMed:11679073}.
CC   -!- SIMILARITY: Belongs to the spo0E family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB13676.1; -; Genomic_DNA.
DR   PIR; F69894; F69894.
DR   RefSeq; NP_389675.1; NC_000964.3.
DR   RefSeq; WP_010886518.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31819; -.
DR   SMR; O31819; -.
DR   STRING; 224308.BSU17920; -.
DR   PaxDb; O31819; -.
DR   PRIDE; O31819; -.
DR   EnsemblBacteria; CAB13676; CAB13676; BSU_17920.
DR   GeneID; 938818; -.
DR   KEGG; bsu:BSU17920; -.
DR   PATRIC; fig|224308.43.peg.1898; -.
DR   OMA; VMTNGMT; -.
DR   BioCyc; BSUB:BSU17920-MON; -.
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; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome; Sporulation.
FT   CHAIN           1..57
FT                   /note="Aspartyl-phosphate phosphatase YnzD"
FT                   /id="PRO_0000359938"
SQ   SEQUENCE   57 AA;  6683 MW;  CECBE66AB1178979 CRC64;
     MIREHLLKEI EKKRAELLQI VMANGMTSHI TIELSQELDH LLIQYQKQRL RAVAGDE