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Serine/threonine-protein kinase PrkC (Ser/Thr-protein kinase PrkC) (EC 2.7.11.1)

 PRKC_BACSU              Reviewed;         648 AA.
O34507;
04-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
07-JUN-2017, entry version 128.
RecName: Full=Serine/threonine-protein kinase PrkC;
Short=Ser/Thr-protein kinase PrkC;
EC=2.7.11.1;
Name=prkC; Synonyms=yloP; OrderedLocusNames=BSU15770;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Foulger D., Errington J.;
"DNA sequence of a 28 Kbp seqment of DNA from the spoVM region of
Bacillus subtilis.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
FUNCTION.
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=12399479; DOI=10.1128/JB.184.22.6109-6114.2002;
Gaidenko T.A., Kim T.-J., Price C.W.;
"The PrpC serine-threonine phosphatase and PrkC kinase have opposing
physiological roles in stationary-phase Bacillus subtilis cells.";
J. Bacteriol. 184:6109-6114(2002).
[4]
FUNCTION, SUBUNIT, DOMAIN, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-40.
STRAIN=168;
PubMed=12406230; DOI=10.1046/j.1365-2958.2002.03178.x;
Madec E., Laszkiewicz A., Iwanicki A., Obuchowski M., Seror S.;
"Characterization of a membrane-linked Ser/Thr protein kinase in
Bacillus subtilis, implicated in developmental processes.";
Mol. Microbiol. 46:571-586(2002).
[5]
PHOSPHORYLATION AT THR-162; THR-163; THR-165; THR-167; SER-214;
THR-290; THR-313 AND THR-320, MUTAGENESIS OF THR-162; THR-163;
THR-165; THR-167; SER-214; THR-290; THR-313 AND THR-320, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12842463; DOI=10.1016/S0022-2836(03)00579-5;
Madec E., Stensballe A., Kjellstrom S., Cladiere L., Obuchowski M.,
Jensen O.N., Seror S.J.;
"Mass spectrometry and site-directed mutagenesis identify several
autophosphorylated residues required for the activity of PrkC, a
Ser/Thr kinase from Bacillus subtilis.";
J. Mol. Biol. 330:459-472(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=168;
PubMed=17218307; DOI=10.1074/mcp.M600464-MCP200;
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
Mann M.;
"The serine/threonine/tyrosine phosphoproteome of the model bacterium
Bacillus subtilis.";
Mol. Cell. Proteomics 6:697-707(2007).
[7]
FUNCTION IN PEPTIDOGLYCAN-DEPENDENT GERMINATION, DISRUPTION PHENOTYPE,
PEPTIDOGLYCAN-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-40.
STRAIN=168 / PY79;
PubMed=18984160; DOI=10.1016/j.cell.2008.08.039;
Shah I.M., Laaberki M.H., Popham D.L., Dworkin J.;
"A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in
response to peptidoglycan fragments.";
Cell 135:486-496(2008).
[8]
3D-STRUCTURE MODELING OF 6-269 IN COMPLEX WITH ATP ANALOGS.
DOI=10.1002/qsar.200730081;
Gruszczyski P., Kamierkiewicz R., Obuchowski M., Lammek B.;
"Theoretical modeling of PrkCc, serine-threonine protein kinase
intracellular domain, complexed with ATP derivatives.";
QSAR Comb. Sci. 27:437-444(2008).
[9]
FUNCTION, SUBSTRATE SPECIFICITY, ENZYME REGULATION, AND MUTAGENESIS OF
LYS-40.
STRAIN=168;
PubMed=19246764; DOI=10.1099/mic.0.022475-0;
Absalon C., Obuchowski M., Madec E., Delattre D., Holland I.B.,
Seror S.J.;
"CpgA, EF-Tu and the stressosome protein YezB are substrates of the
Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.";
Microbiology 155:932-943(2009).
[10]
3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
PubMed=20563625; DOI=10.1007/s10822-010-9370-4;
Gruszczynski P., Obuchowski M., Kazmierkiewicz R.;
"Phosphorylation and ATP-binding induced conformational changes in the
PrkC, Ser/Thr kinase from B. subtilis.";
J. Comput. Aided Mol. Des. 24:733-747(2010).
-!- FUNCTION: Protein kinase that is responsible for triggering spore
germination in response to muropeptides, signaling bacteria to
exit dormancy. PrkC is thus a germination receptor that binds
peptidoglycan fragments containing m-Dpm (meso-diaminopimelate),
which act as spore germinants. Autophosphorylates and
phosphorylates EF-G (elongation factor G, fusA); the latter
modification is likely necessary for germination in response to
peptidoglycan (PubMed:12399479). Another group did not detect
phosphorylation of EF-G (PubMed:19246764). PrkC is a substrate in
vitro of the cotranscribed phosphatase PrpC, which suggests that
they form a functional couple in vivo. Might also be involved in
sporulation and biofilm formation. Does not seem to be involved in
stress response. {ECO:0000269|PubMed:12399479,
ECO:0000269|PubMed:12406230, ECO:0000269|PubMed:18984160,
ECO:0000269|PubMed:19246764}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Bryostatin activates PrkC activity and induces
germination, whereas staurosporine inhibits PrkC and significantly
reduced peptidoglycan-dependent germination. Kinase activity of
isolated N-terminus stimulated by poly-L-lysine or myelin basic
protein (PubMed:19246764). {ECO:0000269|PubMed:19246764}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12406230}.
-!- INTERACTION:
P37562:yabT; NbExp=2; IntAct=EBI-6667154, EBI-9303331;
O31435:ybdM; NbExp=3; IntAct=EBI-6667154, EBI-5255200;
P96716:ywqD; NbExp=2; IntAct=EBI-6667154, EBI-9302929;
-!- SUBCELLULAR LOCATION: Spore core membrane
{ECO:0000269|PubMed:18984160}; Single-pass type II membrane
protein {ECO:0000269|PubMed:18984160}. Note=Is associated with the
inner membrane of the spore.
-!- DOMAIN: The cytoplasmic domain has Ser/Thr kinase activity
(PubMed:12406230). The C-terminal extracellular domain containing
the PASTA repeats binds peptidoglycan.
{ECO:0000269|PubMed:12406230}.
-!- PTM: Autophosphorylation on threonine residue(s) and serine
residue considerably increases the kinase activity of the protein.
Dephosphorylated in vitro by PrpC. {ECO:0000269|PubMed:12406230,
ECO:0000269|PubMed:12842463, ECO:0000269|PubMed:17218307}.
-!- DISRUPTION PHENOTYPE: Spores lacking this gene fail to germinate
in the presence of peptidoglycan fragments or purified GlcNAc-
MurNAc tripeptides and tetrapeptides. They still respond to the
nutrient germinant L-alanine and to the chemical germinant Ca(2+)-
dipicolinic acid, indicating that the spores are still capable of
germinating and that PrkC is not involved in nutrient or chemical
germination. {ECO:0000269|PubMed:18984160}.
-!- MISCELLANEOUS: PubMed:18984160 shows that peptidoglycan fragments
serve as a novel mechanism of interspecies bacterial signaling
that likely indicates the presence of growing bacteria and thus
serve as a signal for dormant cells that growth-promoting
conditions exist.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Y13937; CAA74267.1; -; Genomic_DNA.
EMBL; AL009126; CAB13450.1; -; Genomic_DNA.
PIR; H69878; H69878.
RefSeq; NP_389459.1; NC_000964.3.
RefSeq; WP_003232062.1; NZ_JNCM01000035.1.
ProteinModelPortal; O34507; -.
SMR; O34507; -.
IntAct; O34507; 8.
STRING; 224308.Bsubs1_010100008706; -.
iPTMnet; O34507; -.
PaxDb; O34507; -.
EnsemblBacteria; CAB13450; CAB13450; BSU15770.
GeneID; 936132; -.
KEGG; bsu:BSU15770; -.
PATRIC; fig|224308.179.peg.1717; -.
eggNOG; ENOG4105D9P; Bacteria.
eggNOG; COG0515; LUCA.
eggNOG; COG2815; LUCA.
HOGENOM; HOG000037186; -.
InParanoid; O34507; -.
KO; K12132; -.
OMA; ICAKAMA; -.
PhylomeDB; O34507; -.
BioCyc; BSUB:BSU15770-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0071224; P:cellular response to peptidoglycan; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
GO; GO:0009847; P:spore germination; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR005543; PASTA_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF03793; PASTA; 3.
Pfam; PF00069; Pkinase; 1.
SMART; SM00740; PASTA; 3.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51178; PASTA; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Germination; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 648 Serine/threonine-protein kinase PrkC.
/FTId=PRO_0000171183.
TOPO_DOM 1 330 Cytoplasmic. {ECO:0000305}.
TRANSMEM 331 351 Helical. {ECO:0000255}.
TOPO_DOM 352 648 Extracellular. {ECO:0000305}.
DOMAIN 11 271 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12406230}.
DOMAIN 356 424 PASTA 1. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 425 492 PASTA 2. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 493 559 PASTA 3. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
NP_BIND 17 25 ATP. {ECO:0000305}.
ACT_SITE 134 134 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 40 40 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 40 40 Required for activity.
MOD_RES 162 162 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12842463}.
MOD_RES 163 163 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12842463}.
MOD_RES 165 165 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12842463}.
MOD_RES 167 167 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12842463}.
MOD_RES 214 214 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12842463}.
MOD_RES 290 290 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12842463,
ECO:0000269|PubMed:17218307}.
MOD_RES 313 313 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12842463}.
MOD_RES 320 320 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 40 40 K->A: Does not support germination in
response to peptidoglycan.
{ECO:0000269|PubMed:12406230,
ECO:0000269|PubMed:18984160}.
MUTAGEN 40 40 K->R: Abolishes autophosphorylation and
decreases spore production and biofilm
formation. No phosphorylation of YezB.
{ECO:0000269|PubMed:12406230,
ECO:0000269|PubMed:18984160,
ECO:0000269|PubMed:19246764}.
MUTAGEN 162 162 T->A: 4-fold reduction in activity.
Abolished activity; when associated with
A-163; A-165 and A-167.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 163 163 T->A: 4-fold reduction in activity.
Abolished activity; when associated with
A-162; A-165 and A-167.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 165 165 T->A: 4-fold reduction in activity.
Abolished activity; when associated with
A-162; A-163 and A-167.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 167 167 T->A: 4-fold reduction in activity.
Abolished activity; when associated with
A-162; A-163 and A-165.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 214 214 S->A: 4-fold reduction in activity.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 290 290 T->A: Slightly reduced activity.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 313 313 T->A: Unchanged activity.
{ECO:0000269|PubMed:12842463}.
MUTAGEN 320 320 T->A: 2-fold reduction in activity.
{ECO:0000269|PubMed:12842463}.
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


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