ID A0A101FPM0_9FIRM Unreviewed; 353 AA.
AC A0A101FPM0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 03-MAY-2023, entry version 29.
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=XD69_1063 {ECO:0000313|EMBL:KUK40887.1};
OS Clostridia bacterium 62_21.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1635276 {ECO:0000313|EMBL:KUK40887.1, ECO:0000313|Proteomes:UP000067139};
RN [1] {ECO:0000313|EMBL:KUK40887.1, ECO:0000313|Proteomes:UP000067139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62_21 {ECO:0000313|EMBL:KUK40887.1};
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK40887.1}.
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DR EMBL; LGFR01000110; KUK40887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FPM0; -.
DR PATRIC; fig|1635276.4.peg.226; -.
DR Proteomes; UP000067139; 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 23..255
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT MOTIF 338..343
FT /note="RDXXRA motif of the pArg binding pocket involved in
FT allosteric regulation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00602"
FT BINDING 26..30
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 92
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 126
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 177..181
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 208..213
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 353 AA; 39539 MW; A6F599A29AD40363 CRC64;
MALKDTLTNA YSAWMGAGPE DDVAVSSRVR LARALAHFPF PHRLRREKAE EVIHAVALAV
RQPEVVRKVG RLELVRMTEL SPIERQILVE KHLISPELTR EAEKRAVVLS EDETTSIMVN
EEDHLRIQCL LPGLQLEETW QVADTVDTAL QSVLAFAASE KLGFLTACPT NVGTGLRASV
MLHLPALAMA QQIKETLTAV AKLGLVVRGL YGEGTEAKGN FFQISNQITL GQTEDEIIAN
LVSVTRRVIA QERTARQALY RERREMLEDR VCRAYGALRH ARMISSEEAL RLLSDVRLGI
DLGVIQGVPR RVLTELMIMT RPAFLVKLAG KDLPPFPRDV YRAQLIREKL KQF
//
