ID E7C441_9BACT Unreviewed; 369 AA.
AC E7C441;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 28-JUN-2023, entry version 41.
DE SubName: Full=Arginine kinase {ECO:0000313|EMBL:ADI22215.1};
OS uncultured Gemmatimonadales bacterium HF0200_34B24.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC environmental samples.
OX NCBI_TaxID=723613 {ECO:0000313|EMBL:ADI22215.1};
RN [1] {ECO:0000313|EMBL:ADI22215.1}
RP NUCLEOTIDE SEQUENCE.
RA Pham V.D., Delong E.F.;
RT "Genome fragments of uncultured bacteria from the North Pacific subtropical
RT Gyre.";
RL Submitted (JAN-2010) 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; GU567979; ADI22215.1; -; Genomic_DNA.
DR AlphaFoldDB; E7C441; -.
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 CDD; cd07930; bacterial_phosphagen_kinase; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR023660; Arg_Kinase.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 18..252
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 21..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 369 AA; 40640 MW; 3941F187ED69C127 CRC64;
MPDYGLSWLE ASGDHPDIVL STRVRLARNL QGHAFGPRAR VNDREAILRL FKGSSGKSDI
LSGGTLLEMP AVALRTRRIL LERRVVTRDL LGDEETGPEQ GTAVHLSGLD PVSVMVNEED
HLRVQSLVSG LRIEQAWRMV DRLDEELGRE LPFAYHNEFG FLTSCPTNVG SGLRASVFIH
LPGLVLTKEI GKVLQGLGQV GLTFRGLYGE GSEVIGNFFQ ISNQTTLGKT EEDLVDHLDK
VARQVIQYEL QARQVLLRDA LGVTEDKVWK AYGLLRYARS LSFEELMNLL SGVRLGLSLK
LLPGLRVYTL NKMMIFTQPA HLEEAAGRDL PSSESDAHRA TYVRRILAAE GEVSADDSAS
GGAELSDQA
//
