AC MF_00602; DC Protein; auto TR HAMAP; MF_00602; -; 1; level=0 XX Names: Prot_Arg_kinase XX ID MCSB DE RecName: Full=Protein-arginine kinase; DE EC=2.7.14.1; GN Name=mcsB; XX case CC -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues CC in a large number of proteins. Is part of the bacterial stress response CC system. Protein arginine phosphorylation has a physiologically CC important role and is involved in the regulation of many critical CC cellular processes, such as protein homeostasis, motility, competence, CC and stringent and stress responses, by regulating gene expression and CC protein activity. else CC -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues CC in proteins. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L- CC arginyl-[protein]; Xref=Rhea:RHEA:43384, Rhea:RHEA-COMP:10532, CC Rhea:RHEA-COMP:10533, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83226, ChEBI:CHEBI:456216; CC EC=2.7.14.1; case CC -!- ACTIVITY REGULATION: Appears to be allosterically activated by the CC binding of pArg-containing polypeptides to the pArg-binding pocket CC localized in the C-terminal domain of McsB. end case CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. XX DR Pfam; PF00217; ATP-gua_Ptrans; 1; trigger=no DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1; trigger=no DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1; trigger=yes XX KW ATP-binding KW Kinase KW Nucleotide-binding KW Transferase case KW Allosteric enzyme end case XX GO GO:0016775; F:phosphotransferase activity, nitrogenous group as acceptor GO GO:0004672; F:protein kinase activity XX FT From: MCSB_BACSU (P37570) FT BINDING 27..31 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [SAT]-[SAT]-[RK]-[VI]-[RK] FT BINDING 176..180 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: R-[AT]-[SK]-[VATL]-[MF] FT BINDING 207..212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [RK]-[GS]-[TIL]-x-[GN]-[ES] FT BINDING 92 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: H FT BINDING 125 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: R FT MOTIF 337..342 FT /note="RDXXRA motif of the pArg binding pocket involved in FT allosteric regulation" FT Tag: Motif; Optional; Condition: R-D-x-x-R-A XX Size: 335-363; Related: None; Template: P37570; P0DMM5; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.27 2022/11/19 //