ID   PRPC_BACSU              Reviewed;         254 AA.
AC   O34779; Q799K9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Protein phosphatase PrpC;
DE            EC=3.1.3.16;
GN   Name=prpC; Synonyms=yloO; OrderedLocusNames=BSU15760;
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=9534248; DOI=10.1099/00221287-144-3-801;
RA   Foulger D., Errington J.;
RT   "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT   genome.";
RL   Microbiology 144:801-805(1998).
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 COFACTOR.
RC   STRAIN=168;
RX   PubMed=10986276; DOI=10.1128/jb.182.19.5634-5638.2000;
RA   Obuchowski M., Madec E., Delattre D., Boel G., Iwanicki A., Foulger D.,
RA   Seror S.J.;
RT   "Characterization of PrpC from Bacillus subtilis, a member of the PPM
RT   phosphatase family.";
RL   J. Bacteriol. 182:5634-5638(2000).
RN   [4]
RP   FUNCTION.
RC   STRAIN=168;
RX   PubMed=12406230; DOI=10.1046/j.1365-2958.2002.03178.x;
RA   Madec E., Laszkiewicz A., Iwanicki A., Obuchowski M., Seror S.;
RT   "Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus
RT   subtilis, implicated in developmental processes.";
RL   Mol. Microbiol. 46:571-586(2002).
RN   [5]
RP   FUNCTION, AND IDENTIFICATION OF SUBSTRATES.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=12399479; DOI=10.1128/jb.184.22.6109-6114.2002;
RA   Gaidenko T.A., Kim T.-J., Price C.W.;
RT   "The PrpC serine-threonine phosphatase and PrkC kinase have opposing
RT   physiological roles in stationary-phase Bacillus subtilis cells.";
RL   J. Bacteriol. 184:6109-6114(2002).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF ASP-234.
RC   STRAIN=168;
RX   PubMed=19246764; DOI=10.1099/mic.0.022475-0;
RA   Absalon C., Obuchowski M., Madec E., Delattre D., Holland I.B., Seror S.J.;
RT   "CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr
RT   kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.";
RL   Microbiology 155:932-943(2009).
CC   -!- FUNCTION: Protein phosphatase that dephosphorylates PrkC and EF-G
CC       (elongation factor G, fusA). prpC and prkC are cotranscribed, which
CC       suggests that they form a functional couple in vivo, PrpC's primary
CC       role being possibly to counter the action of PrkC. May be involved in
CC       sporulation and biofilm formation. Does not seem to be involved in
CC       stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB
CC       (PubMed:19246764). {ECO:0000269|PubMed:10986276,
CC       ECO:0000269|PubMed:12399479, ECO:0000269|PubMed:12406230,
CC       ECO:0000269|PubMed:19246764}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:10986276};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:10986276};
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DR   EMBL; Y13937; CAA74266.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13449.1; -; Genomic_DNA.
DR   PIR; G69878; G69878.
DR   RefSeq; NP_389458.1; NC_000964.3.
DR   RefSeq; WP_003232064.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34779; -.
DR   SMR; O34779; -.
DR   IntAct; O34779; 1.
DR   STRING; 224308.BSU15760; -.
DR   PaxDb; O34779; -.
DR   PRIDE; O34779; -.
DR   EnsemblBacteria; CAB13449; CAB13449; BSU_15760.
DR   GeneID; 935931; -.
DR   KEGG; bsu:BSU15760; -.
DR   PATRIC; fig|224308.179.peg.1716; -.
DR   eggNOG; COG0631; Bacteria.
DR   InParanoid; O34779; -.
DR   OMA; MLNAQFF; -.
DR   PhylomeDB; O34779; -.
DR   BioCyc; BSUB:BSU15760-MON; -.
DR   BRENDA; 3.1.3.16; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome; Sporulation.
FT   CHAIN           1..254
FT                   /note="Protein phosphatase PrpC"
FT                   /id="PRO_0000253340"
FT   DOMAIN          2..243
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         234
FT                   /note="D->A: Loss of dephosphorylation activity."
FT                   /evidence="ECO:0000269|PubMed:19246764"
SQ   SEQUENCE   254 AA;  27674 MW;  A01A30A97B47C86E CRC64;
     MLTALKTDTG KIRQHNEDDA GIFKGKDEFI LAVVADGMGG HLAGDVASKM AVKAMGEKWN
     EAETIPTAPS ECEKWLIEQI LSVNSKIYDH AQAHEECQGM GTTIVCALFT GKTVSVAHIG
     DSRCYLLQDD DFVQVTEDHS LVNELVRTGE ISREDAEHHP RKNVLTKALG TDQLVSIDTR
     SFDIEPGDKL LLCSDGLTNK VEGTELKDIL QSDSAPQEKV NLLVDKANQN GGEDNITAVL
     LELALQVEEG EDQC