ID   PRKC_BACSU              Reviewed;         648 AA.
AC   O34507;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Serine/threonine-protein kinase PrkC;
DE            Short=Ser/Thr-protein kinase PrkC;
DE            EC=2.7.11.1;
GN   Name=prkC; Synonyms=yloP; OrderedLocusNames=BSU15770;
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;
RA   Foulger D., Errington J.;
RT   "DNA sequence of a 28 Kbp seqment of DNA from the spoVM region of Bacillus
RT   subtilis.";
RL   Submitted (AUG-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   FUNCTION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 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   [4]
RP   FUNCTION, SUBUNIT, DOMAIN, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-40.
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   PHOSPHORYLATION AT THR-162; THR-163; THR-165; THR-167; SER-214; THR-290;
RP   THR-313 AND THR-320, MUTAGENESIS OF THR-162; THR-163; THR-165; THR-167;
RP   SER-214; THR-290; THR-313 AND THR-320, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12842463; DOI=10.1016/s0022-2836(03)00579-5;
RA   Madec E., Stensballe A., Kjellstrom S., Cladiere L., Obuchowski M.,
RA   Jensen O.N., Seror S.J.;
RT   "Mass spectrometry and site-directed mutagenesis identify several
RT   autophosphorylated residues required for the activity of PrkC, a Ser/Thr
RT   kinase from Bacillus subtilis.";
RL   J. Mol. Biol. 330:459-472(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
RN   [7]
RP   FUNCTION IN PEPTIDOGLYCAN-DEPENDENT GERMINATION, DISRUPTION PHENOTYPE,
RP   PEPTIDOGLYCAN-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-40.
RC   STRAIN=168 / PY79;
RX   PubMed=18984160; DOI=10.1016/j.cell.2008.08.039;
RA   Shah I.M., Laaberki M.H., Popham D.L., Dworkin J.;
RT   "A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in
RT   response to peptidoglycan fragments.";
RL   Cell 135:486-496(2008).
RN   [8]
RP   3D-STRUCTURE MODELING OF 6-269 IN COMPLEX WITH ATP ANALOGS.
RX   DOI=10.1002/qsar.200730081;
RA   Gruszczyski P., Kamierkiewicz R., Obuchowski M., Lammek B.;
RT   "Theoretical modeling of PrkCc, serine-threonine protein kinase
RT   intracellular domain, complexed with ATP derivatives.";
RL   QSAR Comb. Sci. 27:437-444(2008).
RN   [9]
RP   FUNCTION, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP   LYS-40.
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).
RN   [10]
RP   3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
RX   PubMed=20563625; DOI=10.1007/s10822-010-9370-4;
RA   Gruszczynski P., Obuchowski M., Kazmierkiewicz R.;
RT   "Phosphorylation and ATP-binding induced conformational changes in the
RT   PrkC, Ser/Thr kinase from B. subtilis.";
RL   J. Comput. Aided Mol. Des. 24:733-747(2010).
CC   -!- FUNCTION: Protein kinase that is responsible for triggering spore
CC       germination in response to muropeptides, signaling bacteria to exit
CC       dormancy. PrkC is thus a germination receptor that binds peptidoglycan
CC       fragments containing m-Dpm (meso-diaminopimelate), which act as spore
CC       germinants. Autophosphorylates and phosphorylates EF-G (elongation
CC       factor G, fusA); the latter modification is likely necessary for
CC       germination in response to peptidoglycan (PubMed:12399479). Another
CC       group did not detect phosphorylation of EF-G (PubMed:19246764). PrkC is
CC       a substrate in vitro of the cotranscribed phosphatase PrpC, which
CC       suggests that they form a functional couple in vivo. Might also be
CC       involved in sporulation and biofilm formation. Does not seem to be
CC       involved in stress response. {ECO:0000269|PubMed:12399479,
CC       ECO:0000269|PubMed:12406230, ECO:0000269|PubMed:18984160,
CC       ECO:0000269|PubMed:19246764}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- ACTIVITY REGULATION: Bryostatin activates PrkC activity and induces
CC       germination, whereas staurosporine inhibits PrkC and significantly
CC       reduced peptidoglycan-dependent germination. Kinase activity of
CC       isolated N-terminus stimulated by poly-L-lysine or myelin basic protein
CC       (PubMed:19246764). {ECO:0000269|PubMed:19246764}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12406230}.
CC   -!- INTERACTION:
CC       O34507; P37562: yabT; NbExp=2; IntAct=EBI-6667154, EBI-9303331;
CC       O34507; O31435: ybdM; NbExp=3; IntAct=EBI-6667154, EBI-5255200;
CC       O34507; P96716: ywqD; NbExp=2; IntAct=EBI-6667154, EBI-9302929;
CC   -!- SUBCELLULAR LOCATION: Spore membrane {ECO:0000269|PubMed:18984160};
CC       Single-pass type II membrane protein {ECO:0000269|PubMed:18984160}.
CC       Note=Is associated with the inner membrane of the spore.
CC   -!- DOMAIN: The cytoplasmic domain has Ser/Thr kinase activity
CC       (PubMed:12406230). The C-terminal extracellular domain containing the
CC       PASTA repeats binds peptidoglycan. {ECO:0000269|PubMed:12406230}.
CC   -!- PTM: Autophosphorylation on threonine residue(s) and serine residue
CC       considerably increases the kinase activity of the protein.
CC       Dephosphorylated in vitro by PrpC. {ECO:0000269|PubMed:12406230,
CC       ECO:0000269|PubMed:12842463, ECO:0000269|PubMed:17218307}.
CC   -!- DISRUPTION PHENOTYPE: Spores lacking this gene fail to germinate in the
CC       presence of peptidoglycan fragments or purified GlcNAc-MurNAc
CC       tripeptides and tetrapeptides. They still respond to the nutrient
CC       germinant L-alanine and to the chemical germinant Ca(2+)-dipicolinic
CC       acid, indicating that the spores are still capable of germinating and
CC       that PrkC is not involved in nutrient or chemical germination.
CC       {ECO:0000269|PubMed:18984160}.
CC   -!- MISCELLANEOUS: PubMed:18984160 shows that peptidoglycan fragments serve
CC       as a novel mechanism of interspecies bacterial signaling that likely
CC       indicates the presence of growing bacteria and thus serve as a signal
CC       for dormant cells that growth-promoting conditions exist.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; Y13937; CAA74267.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13450.1; -; Genomic_DNA.
DR   PIR; H69878; H69878.
DR   RefSeq; NP_389459.1; NC_000964.3.
DR   RefSeq; WP_003232062.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34507; -.
DR   SMR; O34507; -.
DR   IntAct; O34507; 8.
DR   STRING; 224308.BSU15770; -.
DR   iPTMnet; O34507; -.
DR   jPOST; O34507; -.
DR   PaxDb; 224308-BSU15770; -.
DR   EnsemblBacteria; CAB13450; CAB13450; BSU_15770.
DR   GeneID; 936132; -.
DR   KEGG; bsu:BSU15770; -.
DR   PATRIC; fig|224308.179.peg.1717; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   InParanoid; O34507; -.
DR   OrthoDB; 9788659at2; -.
DR   PhylomeDB; O34507; -.
DR   BioCyc; BSUB:BSU15770-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0071224; P:cellular response to peptidoglycan; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR   GO; GO:0009847; P:spore germination; IMP:UniProtKB.
DR   CDD; cd06577; PASTA_pknB; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.40.2560; -; 1.
DR   Gene3D; 3.30.10.20; -; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF21160; PrkC-like_PASTA-like; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Germination; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..648
FT                   /note="Serine/threonine-protein kinase PrkC"
FT                   /id="PRO_0000171183"
FT   TOPO_DOM        1..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..648
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          11..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:12406230"
FT   DOMAIN          356..424
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          425..492
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          493..559
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   ACT_SITE        134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         17..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   SITE            40
FT                   /note="Required for activity"
FT   MOD_RES         162
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MOD_RES         163
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MOD_RES         165
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MOD_RES         167
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MOD_RES         214
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MOD_RES         290
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463,
FT                   ECO:0000269|PubMed:17218307"
FT   MOD_RES         313
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MOD_RES         320
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         40
FT                   /note="K->A: Does not support germination in response to
FT                   peptidoglycan."
FT                   /evidence="ECO:0000269|PubMed:12406230,
FT                   ECO:0000269|PubMed:18984160"
FT   MUTAGEN         40
FT                   /note="K->R: Abolishes autophosphorylation and decreases
FT                   spore production and biofilm formation. No phosphorylation
FT                   of YezB."
FT                   /evidence="ECO:0000269|PubMed:12406230,
FT                   ECO:0000269|PubMed:18984160, ECO:0000269|PubMed:19246764"
FT   MUTAGEN         162
FT                   /note="T->A: 4-fold reduction in activity. Abolished
FT                   activity; when associated with A-163; A-165 and A-167."
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         163
FT                   /note="T->A: 4-fold reduction in activity. Abolished
FT                   activity; when associated with A-162; A-165 and A-167."
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         165
FT                   /note="T->A: 4-fold reduction in activity. Abolished
FT                   activity; when associated with A-162; A-163 and A-167."
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         167
FT                   /note="T->A: 4-fold reduction in activity. Abolished
FT                   activity; when associated with A-162; A-163 and A-165."
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         214
FT                   /note="S->A: 4-fold reduction in activity."
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         290
FT                   /note="T->A: Slightly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         313
FT                   /note="T->A: Unchanged activity."
FT                   /evidence="ECO:0000269|PubMed:12842463"
FT   MUTAGEN         320
FT                   /note="T->A: 2-fold reduction in activity."
FT                   /evidence="ECO:0000269|PubMed:12842463"
SQ   SEQUENCE   648 AA;  71866 MW;  9653AB5CFBAA7900 CRC64;
     MLIGKRISGR YQILRVIGGG GMANVYLAED IILDREVAIK ILRFDYANDN EFIRRFRREA
     QSASSLDHPN IVSIYDLGEE DDIYYIVMEY VEGMTLKEYI TANGPLHPKE ALNIMEQIVS
     AIAHAHQNQI VHRDIKPHNI LIDHMGNIKV TDFGIATALS STTITHTNSV LGSVHYLSPE
     QARGGLATKK SDIYALGIVL FELLTGRIPF DGESAVSIAL KHLQAETPSA KRWNPSVPQS
     VENIILKATA KDPFHRYETA EDMEADIKTA FDADRLNEKR FTIQEDEEMT KAIPIIKDEE
     LAKAAGEKEA EVTTAQENKT KKNGKRKKWP WVLLTICLVF ITAGILAVTV FPSLFMPKDV
     KIPDVSGMEY EKAAGLLEKE GLQVDSEVLE ISDEKIEEGL MVKTDPKADT TVKEGATVTL
     YKSTGKAKTE IGDVTGQTVD QAKKALKDQG FNHVTVNEVN DEKNAGTVID QNPSAGTELV
     PSEDQVKLTV SIGPEDITLR DLKTYSKEAA SGYLEDNGLK LVEKEAYSDD VPEGQVVKQK
     PAAGTAVKPG NEVEVTFSLG PEKKPAKTVK EKVKIPYEPE NEGDELQVQI AVDDADHSIS
     DTYEEFKIKE PTERTIELKI EPGQKGYYQV MVNNKVVSYK TIEYPKDE
//