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Database: UniProt
Entry: A0A0S8DPE4_9BACT
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ID   A0A0S8DPE4_9BACT        Unreviewed;       349 AA.
AC   A0A0S8DPE4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 28.
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=AMJ78_10575 {ECO:0000313|EMBL:KPK38057.1};
OS   Omnitrophica WOR_2 bacterium SM23_29.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK38057.1, ECO:0000313|Proteomes:UP000050824};
RN   [1] {ECO:0000313|EMBL:KPK38057.1, ECO:0000313|Proteomes:UP000050824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_29 {ECO:0000313|EMBL:KPK38057.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00602}.
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:KPK38057.1}.
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DR   EMBL; LJUB01000163; KPK38057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8DPE4; -.
DR   PATRIC; fig|1703776.3.peg.2017; -.
DR   Proteomes; UP000050824; 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..252
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   MOTIF           335..340
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         89
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         123
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         174..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         205..210
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   349 AA;  40333 MW;  92659A8DE0100E7B CRC64;
     MKLDDLLKQT GEWLKGIGPN SEMVMSSRIR LARNLAKYPF PHRADKKQLE DVLSDFEKAY
     KRIEYFKGAL YLMIKDLNAL DKQFLIERHL ISREHIRHTE YKAVLISDRE IISVMVNEED
     HLRIQILQSG FNLQDTWQLA NKIDEELDRY LDYAYSNELG FLTCCPTNVG TGLRASCMVQ
     LPSLVITKQI KKVLYAITKL GLTARGLYGE GTEAYGNFFQ ISNQVTLGHS EEEIIDNLER
     IMRQIIEQEN AARSSLLANQ RPLFEDMIWR AYGTLKSAHI ITSNEAINLL SHVRLGMDLG
     IIKDIDRNML NELLIQIQPA HLQKLQGKQL STHERDVTRA ELIRSKFMR
//
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