ID   MCSB_BACC4              Reviewed;         354 AA.
AC   B7HJ19;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Protein-arginine kinase {ECO:0000255|HAMAP-Rule:MF_00602};
DE            EC=2.7.14.1 {ECO:0000255|HAMAP-Rule:MF_00602};
GN   Name=mcsB {ECO:0000255|HAMAP-Rule:MF_00602};
GN   OrderedLocusNames=BCB4264_A0101;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00602}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00602};
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00602}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00602}.
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DR   EMBL; CP001176; ACK62305.1; -; Genomic_DNA.
DR   RefSeq; WP_000050842.1; NC_011725.1.
DR   AlphaFoldDB; B7HJ19; -.
DR   SMR; B7HJ19; -.
DR   EnsemblBacteria; ACK62305; ACK62305; BCB4264_A0101.
DR   GeneID; 67504787; -.
DR   KEGG; bcb:BCB4264_A0101; -.
DR   HOGENOM; CLU_066591_1_0_9; -.
DR   OMA; IIMQERV; -.
DR   Proteomes; UP000007096; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07930; bacterial_phosphagen_kinase; 1.
DR   HAMAP; MF_00602; Prot_Arg_kinase; 1.
DR   InterPro; IPR023660; Arg_Kinase.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; PTHR11547; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..354
FT                   /note="Protein-arginine kinase"
FT                   /id="PRO_1000130108"
FT   DOMAIN          24..254
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   MOTIF           337..342
FT                   /note="RDXXRA motif of the pArg binding pocket involved in
FT                   allosteric regulation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         27..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         176..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         207..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ   SEQUENCE   354 AA;  39869 MW;  C8A17E20CFBB415C CRC64;
     MSLDKIMNEA ISPWMKGDGP DSDIVLSSRI RLARNFKQYQ FSTMQNEEEA QKVQELFKKK
     FINKAVEPFG KFGLLKMNEL TPLQRRVLVE KHLISPNLAG TEYGACLLSE SEHISVMLNE
     EDHIRIQCLF PGLQLSKALQ SANQIDNWIE KEVEYAFDES LGYITSCPTN VGTGLRASVM
     IHLPGLVLTK RISRIIQVIQ KLGLVVRGIY GEGSEALGNI FQVSNQMTLG KSEEDIIADL
     KSVMQQIIQQ EKLARELIVQ NSSIELEDKV YRSYGILANS RLIQSAEAAT CLSDVRLGID
     LGYIKGISRN ILTELMVLTQ PGILQQYAGG PLGPEERDYR RATLIRERLR IEKN