ID MCSB_BACCR Reviewed; 354 AA.
AC Q81J67;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=BC_0101;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues
CC in a large number of proteins. Is part of the bacterial stress response
CC system. Protein arginine phosphorylation has a physiologically
CC important role and is involved in the regulation of many critical
CC cellular processes, such as protein homeostasis, motility, competence,
CC and stringent and stress responses, by regulating gene expression and
CC protein activity. {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; AE016877; AAP07183.1; -; Genomic_DNA.
DR RefSeq; NP_829982.1; NC_004722.1.
DR RefSeq; WP_000050842.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81J67; -.
DR SMR; Q81J67; -.
DR STRING; 226900.BC_0101; -.
DR KEGG; bce:BC0101; -.
DR PATRIC; fig|226900.8.peg.103; -.
DR HOGENOM; CLU_066591_1_0_9; -.
DR OrthoDB; 9791353at2; -.
DR Proteomes; UP000001417; 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 Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 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:SF38; ARGININE KINASE; 1.
DR PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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..354
FT /note="Protein-arginine kinase"
FT /id="PRO_0000212013"
FT DOMAIN 24..254
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT MOTIF 337..342
FT /note="RDXXRA motif of the pArg binding pocket involved in
FT allosteric regulation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 27..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 176..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 207..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ SEQUENCE 354 AA; 39869 MW; C8A17E20CFBB415C CRC64;
MSLDKIMNEA ISPWMKGDGP DSDIVLSSRI RLARNFKQYQ FSTMQNEEEA QKVQELFKKK
FINKAVEPFG KFGLLKMNEL TPLQRRVLVE KHLISPNLAG TEYGACLLSE SEHISVMLNE
EDHIRIQCLF PGLQLSKALQ SANQIDNWIE KEVEYAFDES LGYITSCPTN VGTGLRASVM
IHLPGLVLTK RISRIIQVIQ KLGLVVRGIY GEGSEALGNI FQVSNQMTLG KSEEDIIADL
KSVMQQIIQQ EKLARELIVQ NSSIELEDKV YRSYGILANS RLIQSAEAAT CLSDVRLGID
LGYIKGISRN ILTELMVLTQ PGILQQYAGG PLGPEERDYR RATLIRERLR IEKN
//
