ID   MCSB_LISMF              Reviewed;         340 AA.
AC   Q724I1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=LMOf2365_0243;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT03030.1; -; Genomic_DNA.
DR   RefSeq; WP_010958695.1; NC_002973.6.
DR   AlphaFoldDB; Q724I1; -.
DR   SMR; Q724I1; -.
DR   KEGG; lmf:LMOf2365_0243; -.
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:0016775; F:phosphotransferase activity, nitrogenous group as acceptor; ISS:JCVI.
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; 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; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..340
FT                   /note="Protein-arginine kinase"
FT                   /id="PRO_0000212025"
FT   DOMAIN          21..242
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         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         164..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         195..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ   SEQUENCE   340 AA;  38841 MW;  048A2BC1E728F59B CRC64;
     MNVFEPRLSS WLENAGDDDD VVLSSRIRLA RNLKDEQFPV YEQKEEIVDN IAEVFDDNFT
     LIKMNQISLL QKALLVEKHL ISPYMMNKSE YGAVLLNEEE NVSIMLNEED HLRIQCMTPG
     LRLFDALEAA LQIDGYVEEK LSYAFDKEFG YLTSCVTNIG TGMRASVMVH LPGLVTTKRI
     KSVIEAIRSL GFVVRGIYGE GSMPASNIFQ VSNQVTLGKT ETEIVEDLTQ VMEQIIMQER
     VARTTIKQKF HIALEDRVFR SYGLLMNCRI ISMKEASDAI SDIRLGVELG FFEHISRQKM
     NELVLFSQPA FLRREAGRDM DELEEKVIRA KVIREILGDK