ID   MCSB_STAA1              Reviewed;         335 AA.
AC   A7WYT9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=SAHV_0521;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues
CC       in proteins. {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   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00602}.
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DR   EMBL; AP009324; BAF77404.1; -; Genomic_DNA.
DR   RefSeq; WP_000149502.1; NC_009782.1.
DR   AlphaFoldDB; A7WYT9; -.
DR   SMR; A7WYT9; -.
DR   KEGG; saw:SAHV_0521; -.
DR   HOGENOM; CLU_066591_1_0_9; -.
DR   OMA; IIMQERV; -.
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   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..335
FT                   /note="Protein-arginine kinase"
FT                   /id="PRO_1000025877"
FT   DOMAIN          21..244
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         24..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         166..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         197..202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ   SEQUENCE   335 AA;  38596 MW;  E1AA8D8B9BA0D4BB CRC64;
     MTHNIHDNIS QWMKSNEETP IVMSSRIRLA RNLENHVHPL MYATENDGFR VINEVQDALP
     NFELMRLDQM DQQSKMKMVA KHLISPELIK QPAAAVLVND DESLSVMINE EDHIRIQAMG
     TDTTLQALYN QASSIDDELD RSLDISYDEQ LGYLTTCPTN IGTGMRASVM LHLPGLSIMK
     RMTRIAQTIN RFGYTIRGIY GEGSQVYGHT YQVSNQLTLG KSELEIIETL TEVVNQIIHD
     EKQIRQKLDT YNQLETQDRV FRSLGILQNC RMITMEEASY RLSEVKLGID LNYIELQNFK
     FNELMVAIQS PFLLDEEDDK SVKEKRADIL REHIK