MCSB_CHLPN
ID MCSB_CHLPN Reviewed; 358 AA.
AC Q9Z7K4; Q9JSB9; Q9K2E7;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=CPn_0701, CP_0045, CPj0701, CpB0728;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD18840.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF37938.2; -; Genomic_DNA.
DR EMBL; BA000008; BAA98908.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98657.1; -; Genomic_DNA.
DR PIR; B86578; B86578.
DR PIR; E72045; E72045.
DR PIR; H81618; H81618.
DR RefSeq; NP_224897.1; NC_000922.1.
DR RefSeq; WP_010883339.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7K4; -.
DR SMR; Q9Z7K4; -.
DR STRING; 115711.CP_0045; -.
DR EnsemblBacteria; AAD18840; AAD18840; CPn_0701.
DR EnsemblBacteria; AAF37938; AAF37938; CP_0045.
DR GeneID; 45050755; -.
DR KEGG; cpa:CP_0045; -.
DR KEGG; cpj:karG; -.
DR KEGG; cpn:CPn_0701; -.
DR KEGG; cpt:CpB0728; -.
DR PATRIC; fig|115713.3.peg.775; -.
DR eggNOG; COG3869; Bacteria.
DR HOGENOM; CLU_066591_0_0_0; -.
DR OrthoDB; 904915at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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 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..358
FT /note="Protein-arginine kinase"
FT /id="PRO_0000212019"
FT DOMAIN 23..250
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 26..30
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 203..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT CONFLICT 329
FT /note="D -> N (in Ref. 3; BAA98908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40142 MW; 6CAD60FEC3C7D663 CRC64;
MTLPNDLLET LVKRKESPQA NKVWPVTTFS LARNLSVSKF LPCLSKEQKL EILQFITSHF
NHIEGFGEFI VLPLKDTPLW QKEFLLEHFL LPYDLVGNPE GEALVVSRSG DFLAAINFQD
HLVLHGIDFQ GNVEKTLDQL VQLDSYLHSK LSFAFSSEFG FLTTNPKNCG TGLKSQCFLH
IPALLYSKEF TNLIDEEVEI ITSSLLLGVT GFPGNIVVLS NRCSLGLTEE LLLSSLRITA
SKLSVAEVAA KKRLSEENSG DLKNLILRSL GLLTHSCQLE LKETLDALSW IQLGIDLGLI
KVTENHPLWN PLFWQIRRAH LALQKQAEDS RDLQKDTISH LRASVLKELT KGLSPESF
