ID   RSBU_BACSU              Reviewed;         335 AA.
AC   P40399;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Phosphoserine phosphatase RsbU;
DE            EC=3.1.3.3;
DE   AltName: Full=Sigma factor SigB regulation protein RsbU;
GN   Name=rsbU; OrderedLocusNames=BSU04700;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8002610; DOI=10.1128/jb.177.1.123-133.1995;
RA   Wise A.A., Price C.W.;
RT   "Four additional genes in the sigB operon of Bacillus subtilis that control
RT   activity of the general stress factor sigma B in response to environmental
RT   signals.";
RL   J. Bacteriol. 177:123-133(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BSA46;
RX   PubMed=8002609; DOI=10.1128/jb.177.1.114-122.1995;
RA   Voelker U., Dufour A., Haldenwang W.G.;
RT   "The Bacillus subtilis rsbU gene product is necessary for RsbX-dependent
RT   regulation of sigma B.";
RL   J. Bacteriol. 177:114-122(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   FUNCTION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8824586; DOI=10.1101/gad.10.18.2265;
RA   Yang X., Kang C.M., Brody M.S., Price C.W.;
RT   "Opposing pairs of serine protein kinases and phosphatases transmit signals
RT   of environmental stress to activate a bacterial transcription factor.";
RL   Genes Dev. 10:2265-2275(1996).
RN   [6]
RP   ACTIVITY REGULATION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=9786195; DOI=10.1046/j.1365-2958.1998.01052.x;
RA   Kang C.M., Vijay K., Price C.W.;
RT   "Serine kinase activity of a Bacillus subtilis switch protein is required
RT   to transduce environmental stress signals but not to activate its target
RT   PP2C phosphatase.";
RL   Mol. Microbiol. 30:189-196(1998).
RN   [7]
RP   CRYSTALLIZATION OF N-TERMINAL DOMAIN, AND PROTEIN SEQUENCE OF 112-121.
RX   PubMed=12499568; DOI=10.1107/s0907444902020723;
RA   Dutta S., Lewis R.J.;
RT   "Crystallization and preliminary crystallographic analysis of the kinase-
RT   recruitment domain of the PP2C-type phosphatase RsbU.";
RL   Acta Crystallogr. D 59:191-193(2003).
CC   -!- FUNCTION: Positive regulator of sigma-B activity. Dephosphorylates RsbV
CC       in response to environmental stress conveyed from the RsbXST module.
CC       {ECO:0000269|PubMed:8824586}.
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   -!- ACTIVITY REGULATION: Stimulated by a long-lived interaction with RsbT.
CC       {ECO:0000269|PubMed:9786195}.
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DR   EMBL; L35574; AAA85083.1; -; Genomic_DNA.
DR   EMBL; X81652; CAB57214.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB001488; BAA19307.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12277.1; -; Genomic_DNA.
DR   PIR; H69701; H69701.
DR   RefSeq; NP_388351.1; NC_000964.3.
DR   RefSeq; WP_003234295.1; NZ_JNCM01000031.1.
DR   PDB; 1W53; X-ray; 1.60 A; A=1-84.
DR   PDB; 2J6Y; X-ray; 1.85 A; A/B/C/D/E=1-111.
DR   PDB; 2J6Z; X-ray; 1.95 A; A=1-111.
DR   PDB; 2J70; X-ray; 1.95 A; A=1-111.
DR   PDBsum; 1W53; -.
DR   PDBsum; 2J6Y; -.
DR   PDBsum; 2J6Z; -.
DR   PDBsum; 2J70; -.
DR   AlphaFoldDB; P40399; -.
DR   SMR; P40399; -.
DR   DIP; DIP-410N; -.
DR   STRING; 224308.BSU04700; -.
DR   PaxDb; 224308-BSU04700; -.
DR   DNASU; 939939; -.
DR   EnsemblBacteria; CAB12277; CAB12277; BSU_04700.
DR   GeneID; 939939; -.
DR   KEGG; bsu:BSU04700; -.
DR   PATRIC; fig|224308.179.peg.498; -.
DR   eggNOG; COG2208; Bacteria.
DR   InParanoid; P40399; -.
DR   OrthoDB; 311592at2; -.
DR   PhylomeDB; P40399; -.
DR   BioCyc; BSUB:BSU04700-MONOMER; -.
DR   BRENDA; 3.1.3.3; 658.
DR   EvolutionaryTrace; P40399; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1240.30; KaiA/RbsU domain; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR017944; KaiA/RbsU_helical_domain_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR014787; PSer_Pase_RsbU_N.
DR   PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR   PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR   Pfam; PF08673; RsbU_N; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SUPFAM; SSF101215; KaiA/RbsU domain; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..335
FT                   /note="Phosphoserine phosphatase RsbU"
FT                   /id="PRO_0000057790"
FT   DOMAIN          123..333
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   CONFLICT        323
FT                   /note="H -> Q (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2..21
FT                   /evidence="ECO:0007829|PDB:1W53"
FT   HELIX           24..39
FT                   /evidence="ECO:0007829|PDB:1W53"
FT   HELIX           44..58
FT                   /evidence="ECO:0007829|PDB:1W53"
FT   HELIX           64..83
FT                   /evidence="ECO:0007829|PDB:1W53"
SQ   SEQUENCE   335 AA;  38631 MW;  5BD37C05B1A930E3 CRC64;
     MDFREVIEQR YHQLLSRYIA ELTETSLYQA QKFSRKTIEH QIPPEEIISI HRKVLKELYP
     SLPEDVFHSL DFLIEVMIGY GMAYQEHQTL RGIQQEIKSE IEIAANVQQT LLGTKVPQEE
     ALDIGAISVP AKQMSGDYYH FVKDKESINI AIADVIGKGI PAALCMSMIK YAMDSLPETG
     IHPSQVLKNL NRVVEQNVDA SMFITMFYAN YNMDKHQFTY ASAGHEPGFY YSQKDNTFYD
     LEAKGLVLGI SQDYDYKQFD QHLEKGDMIV LFSDGVTECR TENGFLERPD LQKLIEEHMC
     SSAQEMVKNI YDSLLKLQDF QLHDDFTLIV LRRKV
//