ID   RAPB_BACSU              Reviewed;         377 AA.
AC   P70962;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Response regulator aspartate phosphatase B;
DE            EC=3.1.-.-;
DE   AltName: Full=Stage 0 sporulation protein P;
GN   Name=rapB; Synonyms=spo0P, ywmE; OrderedLocusNames=BSU36690;
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=8001132; DOI=10.1016/0092-8674(94)90035-3;
RA   Perego M., Hanstein C., Welsh K., Djavakhishvili T., Glaser P., Hoch J.;
RT   "Multiple protein-aspartate phosphatases provide a mechanism for the
RT   integration of diverse signals in the control of development in B.
RT   subtilis.";
RL   Cell 79:1047-1055(1994).
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).
CC   -!- FUNCTION: Prevents sporulation by dephosphorylating Spo0F.
CC   -!- SIMILARITY: Belongs to the RAP family. {ECO:0000305}.
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DR   EMBL; Z81356; CAB03684.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15686.1; -; Genomic_DNA.
DR   PIR; E69688; E69688.
DR   RefSeq; NP_391550.1; NC_000964.3.
DR   RefSeq; WP_003227715.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P70962; -.
DR   SMR; P70962; -.
DR   STRING; 224308.BSU36690; -.
DR   PaxDb; P70962; -.
DR   PRIDE; P70962; -.
DR   EnsemblBacteria; CAB15686; CAB15686; BSU_36690.
DR   GeneID; 936963; -.
DR   KEGG; bsu:BSU36690; -.
DR   PATRIC; fig|224308.179.peg.3972; -.
DR   eggNOG; COG0457; Bacteria.
DR   InParanoid; P70962; -.
DR   OMA; FLTYYYH; -.
DR   PhylomeDB; P70962; -.
DR   BioCyc; BSUB:BSU36690-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR041617; TPR_MalT.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protein phosphatase; Reference proteome; Repeat; Sporulation;
KW   TPR repeat.
FT   CHAIN           1..377
FT                   /note="Response regulator aspartate phosphatase B"
FT                   /id="PRO_0000106436"
FT   REPEAT          100..133
FT                   /note="TPR 1"
FT   REPEAT          147..180
FT                   /note="TPR 2"
FT   REPEAT          181..214
FT                   /note="TPR 3"
FT   REPEAT          221..254
FT                   /note="TPR 4"
FT   REPEAT          260..293
FT                   /note="TPR 5"
FT   REPEAT          335..368
FT                   /note="TPR 6"
SQ   SEQUENCE   377 AA;  45037 MW;  617B29614B483971 CRC64;
     MAAYEIPSSQ VGVKINKWYK HILAFQVADA VKLKEEIDLD IEQMEEDQLL LLYYQLISYR
     HQIMLDYVKP DLHEESQLQY RELIKTLESN QDSISGLSEY YFHLFRGMYE FEQNNYISAI
     SFYRKAEKML AFVEDEIERA EFHFKVAEVF YIMKQTHFSM NHAVQALETY KAHDFYRVRR
     IQCHFVISGN YIDYRNYEKA LEHLDDAYRL ALLEGQPRLI GSALYNIGNC YDDKGELDQA
     AEYFEKALPV FEDYQLEQLP KALFSLTRVL FKKQDSEAAI RYYEKGIAIA QKRNDFFSLA
     KYKFLQALYV ESVNLNMIQE VFDYMEEKGL YVYIEEFALD AASYFSHREQ YKEAVYFYEK
     AVSMREMIQR NDCLYEV