MCSB_CLOK5
ID MCSB_CLOK5 Reviewed; 345 AA.
AC A5N4L9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=CKL_0194;
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK32250.1; -; Genomic_DNA.
DR RefSeq; WP_011988776.1; NC_009706.1.
DR AlphaFoldDB; A5N4L9; -.
DR SMR; A5N4L9; -.
DR STRING; 431943.CKL_0194; -.
DR EnsemblBacteria; EDK32250; EDK32250; CKL_0194.
DR KEGG; ckl:CKL_0194; -.
DR eggNOG; COG3869; Bacteria.
DR HOGENOM; CLU_066591_1_0_9; -.
DR OMA; IIMQERV; -.
DR OrthoDB; 904915at2; -.
DR Proteomes; UP000002411; 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..345
FT /note="Protein-arginine kinase"
FT /id="PRO_1000082502"
FT DOMAIN 15..245
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT MOTIF 328..333
FT /note="RDXXRA motif of the pArg binding pocket involved in
FT allosteric regulation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 18..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 167..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 198..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ SEQUENCE 345 AA; 39135 MW; CCBE805E843CF691 CRC64;
MNNWVTTYEN HNYGLVISSR IRLARNLAKI PFSHKLNIEE SKKVIKNVEN AFYTFSNTEE
KFKSNYLWDK NDNEKNIYLE KHLISKNLID NSSKAAFILD DKETISIMIN EEDHVRIQCI
TGGLNLEEVY DVSEKIDDLL EENLEYAFDE KLGYLTACPT NVGTGLRASV MLHLPSLSLN
NQINGFLNAL AQVGMTIRGL YGEGSKAIGN IYQISNQVTL GRSEEEILSN LKALVLQIIN
QEIISRENLM KKYKYELEDK IYRALGVLKS AVLLNSSECL KLLSDVRLGV EMGIIKDVNG
ITLNKLLVES QPATIQKIYG ESLSNKDRDF NRAKFVREKL AVNTA
