ID   RSBP_BACSU              Reviewed;         403 AA.
AC   O07014;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Phosphoserine phosphatase RsbP;
DE            EC=3.1.3.3;
GN   Name=rsbP; Synonyms=yvfP; OrderedLocusNames=BSU34110;
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   Denizot F.;
RL   Submitted (APR-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   CHARACTERIZATION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=10632888; DOI=10.1046/j.1365-2958.2000.01697.x;
RA   Vijay K., Brody M.S., Fredlund E., Price C.W.;
RT   "A PP2C phosphatase containing a PAS domain is required to convey signals
RT   of energy stress to the sigmaB transcription factor of Bacillus subtilis.";
RL   Mol. Microbiol. 35:180-188(2000).
CC   -!- FUNCTION: Positive regulator of sigma-B activity. Dephosphorylates RsbV
CC       in response to energy stress.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC         Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC         Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- INDUCTION: Induced by entry into stationary phase, but not by carbon
CC       and energy starvation.
CC   -!- DOMAIN: The PAS domain may participate in sensing the overall energy
CC       level of the cell and communicate this information to the phosphatase
CC       domain.
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DR   EMBL; Z94043; CAB08010.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15416.1; -; Genomic_DNA.
DR   PIR; G70038; G70038.
DR   RefSeq; NP_391291.1; NC_000964.3.
DR   RefSeq; WP_003228290.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O07014; -.
DR   SMR; O07014; -.
DR   STRING; 224308.BSU34110; -.
DR   PaxDb; O07014; -.
DR   PRIDE; O07014; -.
DR   EnsemblBacteria; CAB15416; CAB15416; BSU_34110.
DR   GeneID; 936673; -.
DR   KEGG; bsu:BSU34110; -.
DR   PATRIC; fig|224308.179.peg.3698; -.
DR   eggNOG; COG2208; Bacteria.
DR   InParanoid; O07014; -.
DR   OMA; HYCTAIY; -.
DR   PhylomeDB; O07014; -.
DR   BioCyc; BSUB:BSU34110-MON; -.
DR   BRENDA; 3.1.3.3; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Protein phosphatase; Reference proteome.
FT   CHAIN           1..403
FT                   /note="Phosphoserine phosphatase RsbP"
FT                   /id="PRO_0000057789"
FT   DOMAIN          1..42
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          191..402
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
SQ   SEQUENCE   403 AA;  46030 MW;  104A3651F7FC7962 CRC64;
     MDKQLNDAPC GFLALSEEGS IIAANRTLIK ILDYEPEQVI GQHMNMMLTI PAQLFCQLYF
     FPLLKLEHHI EEIYISLKAR DGEEIPVLIN AIARHDSGAS VFDCVLIPMR KRNEYENELL
     IARNEAQEAL LAKQKANAEL EIALETLKAK QEELLEINKQ NQQFKLNTKR ELELARKIQK
     NSLTEPIVND QVQIDSYYNA SSELSGDLYG YYQIDEHRYG IIILDVMGHG ISSALITMSL
     HPLFQRQITQ GLSPVKVMKE LDRHLHSLFQ NDEEARHYCT AIYLEIDIAR QRIDYVNAGH
     PPALWQDDSG TQHLLHATSP PIGMFEDLEF QSSSLSYTED GRLLLYTDGV MDPTASCYLF
     DLLKDHPDSP IADLKEKILT SLQHQKEAHH KSDDECFILV DVK