##gff-version 3
O34507	UniProtKB	Chain	1	648	.	.	.	ID=PRO_0000171183;Note=Serine/threonine-protein kinase PrkC	
O34507	UniProtKB	Topological domain	1	330	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O34507	UniProtKB	Transmembrane	331	351	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O34507	UniProtKB	Topological domain	352	648	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O34507	UniProtKB	Domain	11	271	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:12406230;Dbxref=PMID:12406230	
O34507	UniProtKB	Domain	356	424	.	.	.	Note=PASTA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00528	
O34507	UniProtKB	Domain	425	492	.	.	.	Note=PASTA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00528	
O34507	UniProtKB	Domain	493	559	.	.	.	Note=PASTA 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00528	
O34507	UniProtKB	Active site	134	134	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
O34507	UniProtKB	Binding site	17	25	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305	
O34507	UniProtKB	Binding site	40	40	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
O34507	UniProtKB	Site	40	40	.	.	.	Note=Required for activity	
O34507	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Modified residue	214	214	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Modified residue	290	290	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12842463,ECO:0000269|PubMed:17218307;Dbxref=PMID:12842463,PMID:17218307	
O34507	UniProtKB	Modified residue	313	313	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Does not support germination in response to peptidoglycan. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12406230,ECO:0000269|PubMed:18984160;Dbxref=PMID:12406230,PMID:18984160	
O34507	UniProtKB	Mutagenesis	40	40	.	.	.	Note=Abolishes autophosphorylation and decreases spore production and biofilm formation. No phosphorylation of YezB. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12406230,ECO:0000269|PubMed:18984160,ECO:0000269|PubMed:19246764;Dbxref=PMID:12406230,PMID:18984160,PMID:19246764	
O34507	UniProtKB	Mutagenesis	162	162	.	.	.	Note=4-fold reduction in activity. Abolished activity%3B when associated with A-163%3B A-165 and A-167. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	163	163	.	.	.	Note=4-fold reduction in activity. Abolished activity%3B when associated with A-162%3B A-165 and A-167. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	165	165	.	.	.	Note=4-fold reduction in activity. Abolished activity%3B when associated with A-162%3B A-163 and A-167. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	167	167	.	.	.	Note=4-fold reduction in activity. Abolished activity%3B when associated with A-162%3B A-163 and A-165. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	214	214	.	.	.	Note=4-fold reduction in activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	290	290	.	.	.	Note=Slightly reduced activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Unchanged activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463	
O34507	UniProtKB	Mutagenesis	320	320	.	.	.	Note=2-fold reduction in activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12842463;Dbxref=PMID:12842463