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Database: UniProt
Entry: A0A090JLS5_9FIRM
LinkDB: A0A090JLS5_9FIRM
Original site: A0A090JLS5_9FIRM 
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
//
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