ID   MCSB_OCEIH              Reviewed;         354 AA.
AC   Q8EU06;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=OB0092;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12048.1; -; Genomic_DNA.
DR   RefSeq; WP_011064495.1; NC_004193.1.
DR   AlphaFoldDB; Q8EU06; -.
DR   SMR; Q8EU06; -.
DR   STRING; 221109.22775770; -.
DR   EnsemblBacteria; BAC12048; BAC12048; BAC12048.
DR   KEGG; oih:OB0092; -.
DR   eggNOG; COG3869; Bacteria.
DR   HOGENOM; CLU_066591_1_0_9; -.
DR   OMA; IIMQERV; -.
DR   OrthoDB; 904915at2; -.
DR   PhylomeDB; Q8EU06; -.
DR   Proteomes; UP000000822; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..354
FT                   /note="Protein-arginine kinase"
FT                   /id="PRO_0000212027"
FT   DOMAIN          24..255
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   MOTIF           338..343
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         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         177..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         208..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ   SEQUENCE   354 AA;  40454 MW;  F6DD3EBD1293844D CRC64;
     MTLDKFIDQA ISPWMREEGP DKDIVMSSRI RLARNFANQT YPILAKEEKL VEIQEFIRDE
     YANKSFQTYK DLQYVPLTDL SPVEKSVLVE KHLISPHLIK HSDFAATLIS ENEQVSIMVN
     EEDHLRIQVY YPGLQLKTAL EQSFALDDWL EEKVDYAFDE TKGYLTSCPT NVGTGMRASV
     MMHLPALVLT KQINRLIPAI SQFGLVVRGI YGEGSEALGN IFQVSNQITL GKSEQDIVDD
     LESVVHQLIE HERMARNHIL ERTGKKLEDR IFRSYGTLAY SRIIDSKEAS KCISDVRLGI
     DLGLIDNTSG NILNELMVLT QPGFLQHYAN RSLRPDERDV LRASVIRERL KLEE