MCSB_CLOBB
ID MCSB_CLOBB Reviewed; 339 AA.
AC B2TIE4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=CLL_A0206;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) 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; CP001056; ACD24219.1; -; Genomic_DNA.
DR RefSeq; WP_012424986.1; NC_018648.1.
DR AlphaFoldDB; B2TIE4; -.
DR SMR; B2TIE4; -.
DR EnsemblBacteria; ACD24219; ACD24219; CLL_A0206.
DR KEGG; cbk:CLL_A0206; -.
DR PATRIC; fig|935198.13.peg.180; -.
DR HOGENOM; CLU_066591_1_0_9; -.
DR OMA; IIMQERV; -.
DR OrthoDB; 904915at2; -.
DR Proteomes; UP000001195; 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; 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..339
FT /note="Protein-arginine kinase"
FT /id="PRO_1000130111"
FT DOMAIN 14..242
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 17..21
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 339 AA; 38992 MW; C9ADED4CE60E8900 CRC64;
MKNWINEECN KEDIVINSNI SLSRNLKEKP FSNKLNEIEA RENVGFIYQI VKSELKDESC
IYQLWNEDKE LINSYLDKQL ISKELIKNKD KTAFVLNSEE TLSIMINEDD HLKLRCITAG
FDLETAFDNI TKLDDKIEKR VHYAFDENLG YLTTSPTNLG TGMRASVNIH LPALNFNDEI
SNFSKGLTQI GMDMKGLYEE GNKAYGNMYK ISNQVTLGLT EEEIIDNLKG AVLNVISEEK
KFREVLLTKC KYDIEDKVFR AYGILTSAIL LSEKECTELL SSVRFGVELS LLDISKNKLN
KLLVYTRDSS LQNYLKRKLS NKELNYERAK FVRAILAQN
