MCSB_BACVZ
ID MCSB_BACVZ Reviewed; 363 AA.
AC A7Z0K7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=RBAM_001100;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS72533.1; -; Genomic_DNA.
DR RefSeq; WP_003156398.1; NC_009725.2.
DR AlphaFoldDB; A7Z0K7; -.
DR SMR; A7Z0K7; -.
DR STRING; 326423.RBAM_001100; -.
DR EnsemblBacteria; ABS72533; ABS72533; RBAM_001100.
DR GeneID; 66327894; -.
DR KEGG; bay:RBAM_001100; -.
DR HOGENOM; CLU_066591_1_0_9; -.
DR OMA; IIMQERV; -.
DR Proteomes; UP000001120; 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; Transferase.
FT CHAIN 1..363
FT /note="Protein-arginine kinase"
FT /id="PRO_1000025868"
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 363 AA; 40965 MW; 985C569622205ABD CRC64;
MSLKHFIQDA LSNWMKQKGP ESDIVLSSRI RLARNFENIK FPARYTNEEA SSIIQQFEDH
FSGKELPDIG QFHLIRMSEA QPLEKRVLME KHLISPNLTE SPFGGCLLSE NEEVSIMLNE
EDHIRIQCLF PGFQLLNAIK AANQVDDWIE EKVDYAFGEK RGYLTSCPTN VGTGLRASVM
MHLPGLVLTR QMNRIIPAIN QLGLVVRGIY GEGSEALGNI FQISNQITLG KSEQDIVDDL
NSVAAQLIEQ ERSAREALYQ TSKIELEDRV FRSYGVLSNC RMIESKETAK CLSDVRLGID
LGIIKGLSSN ILNELMILTQ PGFLQQYSGG ALRPNERDAR RAALIRERLH LEMSANRQED
DSI
