YISI_BACSU
ID YISI_BACSU Reviewed; 56 AA.
AC O06722;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Aspartyl-phosphate phosphatase YisI;
DE EC=3.1.3.-;
DE AltName: Full=Stage 0 sporulation regulatory protein YisI;
GN Name=yisI; OrderedLocusNames=BSU10730;
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=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
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, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y09476; CAA70680.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12913.1; -; Genomic_DNA.
DR PIR; A69837; A69837.
DR RefSeq; NP_388954.1; NC_000964.3.
DR RefSeq; WP_003233086.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O06722; -.
DR SMR; O06722; -.
DR STRING; 224308.BSU10730; -.
DR PaxDb; O06722; -.
DR EnsemblBacteria; CAB12913; CAB12913; BSU_10730.
DR GeneID; 936347; -.
DR KEGG; bsu:BSU10730; -.
DR PATRIC; fig|224308.179.peg.1154; -.
DR eggNOG; ENOG50304QH; Bacteria.
DR OMA; TIECSQE; -.
DR BioCyc; BSUB:BSU10730-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..56
FT /note="Aspartyl-phosphate phosphatase YisI"
FT /id="PRO_0000049582"
SQ SEQUENCE 56 AA; 6673 MW; 02749CD2B6141DB1 CRC64;
MNSKIEEMRI TLIETAQKYG MNSKETIQCS QELDILLNTR IKEEMIFGRY LENSRM