ID A0A150LF66_9BACI Unreviewed; 357 AA.
AC A0A150LF66;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=B4102_0038 {ECO:0000313|EMBL:KYD10978.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD10978.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYD10978.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYD10978.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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: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:KYD10978.1}.
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DR EMBL; LQYN01000010; KYD10978.1; -; Genomic_DNA.
DR RefSeq; WP_066226617.1; NZ_LQYN01000010.1.
DR AlphaFoldDB; A0A150LF66; -.
DR STRING; 46224.B4102_0038; -.
DR PATRIC; fig|46224.3.peg.393; -.
DR OrthoDB; 9791353at2; -.
DR Proteomes; UP000075666; 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|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000075666};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00602}.
FT DOMAIN 24..254
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT MOTIF 337..342
FT /note="RDXXRA motif of the pArg binding pocket involved in
FT allosteric regulation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602"
FT BINDING 27..31
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 91
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 125
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 176..180
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 207..212
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 357 AA; 40138 MW; 9826E54A12E95633 CRC64;
MSLEKFVNQA VSSWMNQEGP NSDIVLSSRV RLARNFKQFN FPTLFSNEEA REIISKVETV
LQSKSFPENN MELLRMEDLQ TLQKKVLVEK HLISPNLADE SSHGAVILTS EEDVSIMINE
EDHIRIQCLF PGLQLKEALE KASKIDDLME EHIDYAFSEK LGYLTSCPTN VGTGMRASVM
VHLPGLVLTQ QMNRVIPAIS QLGLVVRGIY GEGSEALGNI FQISNQITLG KTEIDIVEDL
MSVVQQIIAQ ERSAREALIK TSNIQLEDKV FRSFGVLANS RIIESKEAAQ CLSDLRLGID
MGYIKNVSKN ILNELMILTQ PGFLQQYAGG PLRPHERDIR RATLIRERLK LEEVNNG
//