ID S9TXF9_PAEAL Unreviewed; 368 AA.
AC S9TXF9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Protein-arginine kinase {ECO:0000256|HAMAP-Rule:MF_00602};
DE EC=2.7.14.1 {ECO:0000256|HAMAP-Rule:MF_00602};
GN Name=mcsB {ECO:0000256|HAMAP-Rule:MF_00602};
GN ORFNames=PAALTS15_12182 {ECO:0000313|EMBL:EPY06911.1};
OS Paenibacillus alvei TS-15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1117108 {ECO:0000313|EMBL:EPY06911.1, ECO:0000313|Proteomes:UP000015344};
RN [1] {ECO:0000313|EMBL:EPY06911.1, ECO:0000313|Proteomes:UP000015344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS-15 {ECO:0000313|EMBL:EPY06911.1,
RC ECO:0000313|Proteomes:UP000015344};
RA Strain E.A., Brown E., Allard M.W., Luo Y.L.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues
CC in proteins. {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_00602}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-ProRule:PRU00843,
CC ECO:0000256|RuleBase:RU000505}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPY06911.1}.
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DR EMBL; ATMT01000049; EPY06911.1; -; Genomic_DNA.
DR AlphaFoldDB; S9TXF9; -.
DR PATRIC; fig|1117108.3.peg.2525; -.
DR eggNOG; COG3869; Bacteria.
DR Proteomes; UP000015344; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 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 {ECO:0000256|HAMAP-Rule:MF_00602};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00602};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00602};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00602}.
FT DOMAIN 37..268
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT MOTIF 351..356
FT /note="RDXXRA motif of the pArg binding pocket involved in
FT allosteric regulation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602"
FT BINDING 40..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 190..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 221..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 368 AA; 41277 MW; D72E6EE75C7848B0 CRC64;
MTISSANLEG DDEMTERRFI EEALSDWMRG TGPDSDIVIS SRIRIARNIS GLPFPLLATN
QQSAEVLDRL SAVMKDPEFA QLNHFHELEL AELSDTEKQV LVEKHLISPS LANESRNGAV
IVSEDESTSI MINEEDHLRI QCLFPGLQIR EAWEQANRID DVFESQIDYA FDEKRGFLTS
CPTNVGTGIR ASVMMHLPAL VMTQQINLML QAVTQVGLAV RGIYGEGSEA IGNLFQISNQ
ITLGQSESEI IDNLYSVVKQ LIEHEKAARE QLLTSNSMRL TDRICRSYGI LKHAVIMDSK
EAAQRLSDIR LGSDLGILQH IQSSQLNELL VMTQPGFLQY KYNTTLSAED RDSYRAKMIR
ETLSKSKS
//
