ID A0A090JLS5_9FIRM Unreviewed; 324 AA.
AC A0A090JLS5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative ATP:guanido phosphotransferase domain protein {ECO:0000313|EMBL:CDZ74394.1};
DE EC=2.7.3.- {ECO:0000313|EMBL:CDZ74394.1};
GN ORFNames=ING2D1G_0200 {ECO:0000313|EMBL:CDZ74394.1};
OS Peptoniphilus sp. ING2-D1G.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1912856 {ECO:0000313|EMBL:CDZ74394.1, ECO:0000313|Proteomes:UP000032409};
RN [1] {ECO:0000313|EMBL:CDZ74394.1, ECO:0000313|Proteomes:UP000032409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Peptoniphilus sp. ING2-D1G {ECO:0000313|Proteomes:UP000032409};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU00843}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00843}.
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DR EMBL; LM997412; CDZ74394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090JLS5; -.
DR STRING; 1912856.ING2D1G_0200; -.
DR KEGG; ped:ING2D1G_0200; -.
DR PATRIC; fig|875453.3.peg.194; -.
DR HOGENOM; CLU_066591_0_0_9; -.
DR OrthoDB; 9791353at2; -.
DR Proteomes; UP000032409; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
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; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00843};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00843};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00843}; Reference proteome {ECO:0000313|Proteomes:UP000032409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 3..225
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 6..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 149..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 179..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 324 AA; 37619 MW; 461E2DDE84F5396C CRC64;
MSVILYNELK LSRNVSGLNF PSKIDNESAE RILTKLDYIL SKKEFKLKRT RDLSSLEKLQ
LYEDCVLNAS ILKHEHFSAV FIDENDLVVR VNGDNHIEIY KSTKEKNLPD IFEQINEVDD
YIDDNIKYAF REDFGYLNSN PNYCGNGLVA EVYLHLPAIN YFGRNSLMNT LNRLGYNISS
LNMGDKAVGS IYKLSLDRTI GIDEKEYLSK LINISNEIED MEEQNRKKLY LDEIIDLEDL
VNRAFGILRN SRVIDELEMI DKMSDLFLGI ELSILKPKEK LDLIDSIKQF KNGHLQVERG
ALLDEKSRNI LRANNIRKMM KEVF
//