ID   MCSB_BACCN              Reviewed;         356 AA.
AC   A7GJZ2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=Bcer98_0075;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS20450.1; -; Genomic_DNA.
DR   RefSeq; WP_011983219.1; NC_009674.1.
DR   AlphaFoldDB; A7GJZ2; -.
DR   SMR; A7GJZ2; -.
DR   STRING; 315749.Bcer98_0075; -.
DR   EnsemblBacteria; ABS20450; ABS20450; Bcer98_0075.
DR   GeneID; 56415596; -.
DR   KEGG; bcy:Bcer98_0075; -.
DR   eggNOG; COG3869; Bacteria.
DR   HOGENOM; CLU_066591_1_0_9; -.
DR   OMA; IIMQERV; -.
DR   OrthoDB; 904915at2; -.
DR   Proteomes; UP000002300; 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..356
FT                   /note="Protein-arginine kinase"
FT                   /id="PRO_1000082501"
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   356 AA;  40079 MW;  433E9033DC75A14D CRC64;
     MSLDRIMNEA ISPWMKGDGP DSDIVLSTRI RLARNLKNYH FPIMQTAEEA NQITELFQQK
     LVNKTMRDFG SFELLKMNEL TPLQRRVLVE KHLISPNLAE TEFGACILSE SEHISVMLNE
     EDHVRIQCLF PGLQLSEALQ SANKIDNVFE EVVEYAFDEE LGYVTSCPTN VGTGLRASVM
     IHLPALVLTK RINRIIQAIQ QLGLVVRGIY GEGSEALGNI FQVSNQMTLG KSEEDIIADL
     TSVIHQLIQQ EKAARELIVK NSSIELEDKV YRSYGILAHS RLIQSAEAAT CLSDVRLGID
     LGYIKDVSRN ILTELMVLTQ PGILQQYAGG QLGPEERDYR RAALIRERLR IEENEA