ID   MCSB_CHLTR              Reviewed;         356 AA.
AC   O84682;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, 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=CT_675;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68270.1; -; Genomic_DNA.
DR   PIR; B71484; B71484.
DR   RefSeq; NP_220194.1; NC_000117.1.
DR   RefSeq; WP_009872047.1; NC_000117.1.
DR   AlphaFoldDB; O84682; -.
DR   SMR; O84682; -.
DR   STRING; 813.O172_03715; -.
DR   EnsemblBacteria; AAC68270; AAC68270; CT_675.
DR   GeneID; 884461; -.
DR   KEGG; ctr:CT_675; -.
DR   PATRIC; fig|272561.5.peg.742; -.
DR   HOGENOM; CLU_066591_0_0_0; -.
DR   InParanoid; O84682; -.
DR   OMA; SHFNHIE; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..356
FT                   /note="Protein-arginine kinase"
FT                   /id="PRO_0000212020"
FT   DOMAIN          22..249
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         25..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         172..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         202..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ   SEQUENCE   356 AA;  40244 MW;  47F640A12DAD0A6B CRC64;
     MLPNHILTAI ATIKHSLRTE TPRPICTLSL SRNLSVSKFV PCLSKENKRD VLETIAKQFS
     AIEGEEFFVL PLKDLPIWQR ECLLEHYLFP YHLGSYLEGE ALIVNQAGTL LAGINLRDHL
     VIHGVDFVWQ PEVLLQKLID LDIRLQQSLS FAFSSDFGFL TADPLRCGTA LIARAFVHVP
     ALKYGDALSE LLVPYQREFA SSSLLPLSQE SLGDILCLSN ICSLGLSEEQ ILSSLRLVVS
     KILSAEREAR NQLVKENPTE IKNRILRSVG MLTHSCCLDL QEALDATSWI QLGMSMQWIE
     DSEKHPLWNP LFWDLRRGHL ALYNQDTANR SIEKEVIAQI RAKATKPQAE RLIIRI