ID   MCSB_HALOH              Reviewed;         349 AA.
AC   B8D093;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Hore_00860;
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562;
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
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   -!- 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; CP001098; ACL68847.1; -; Genomic_DNA.
DR   RefSeq; WP_012635046.1; NC_011899.1.
DR   AlphaFoldDB; B8D093; -.
DR   SMR; B8D093; -.
DR   STRING; 373903.Hore_00860; -.
DR   EnsemblBacteria; ACL68847; ACL68847; Hore_00860.
DR   KEGG; hor:Hore_00860; -.
DR   eggNOG; COG3869; Bacteria.
DR   HOGENOM; CLU_066591_1_0_9; -.
DR   OMA; IIMQERV; -.
DR   OrthoDB; 904915at2; -.
DR   Proteomes; UP000000719; 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..349
FT                   /note="Protein-arginine kinase"
FT                   /id="PRO_1000147062"
FT   DOMAIN          24..252
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   MOTIF           335..340
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         89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         174..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         205..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ   SEQUENCE   349 AA;  39109 MW;  73E22A40C69F4EC8 CRC64;
     MSLKDLINKN LSHWVAGQGP ERDIVLSSRI RLARNLDTIP YPNRADKDSK EEVTKRVLDA
     TSKQGKIKLH YIKMDDLPEV EREVLVEKHL ISPAHAKAGE GKGVLLNDNE TISIMINEED
     HLRLQVLIPG LQLEGAWETA SELDDLLEEK LDFAFSQKWG YLSACPTNVG TGLRASVMVH
     LPALNLTNNI NKMLGAISKV GLTVRGIYGE GSEYVGNLYQ ISNQVTLGHT EKEIIANLKS
     VTSQIIEQER QARNLLLKEK EIEVRDRVNR SFGILSHAYQ ISSEEALRML SNVKLGIDMG
     IITDVDTGVL SELMVLIRPA HLQKLEGKEL TPTERDIKRA ELIKTRLNM