PRKC_BACSU
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 03-AUG-2022, entry version 150.
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; Firmicutes; 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 / 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 [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; O34507; -.
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 OMA; DPDYRYQ; -.
DR PhylomeDB; O34507; -.
DR BioCyc; BSUB:BSU15770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 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 Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
