ID G5KBX2_9STRE Unreviewed; 303 AA.
AC G5KBX2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Lipid kinase, YegS/Rv2252/BmrU family {ECO:0000313|EMBL:EHI64872.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:EHI64872.1};
GN ORFNames=STRPS_1845 {ECO:0000313|EMBL:EHI64872.1};
OS Streptococcus pseudoporcinus LQ 940-04.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=875093 {ECO:0000313|EMBL:EHI64872.1, ECO:0000313|Proteomes:UP000003217};
RN [1] {ECO:0000313|EMBL:EHI64872.1, ECO:0000313|Proteomes:UP000003217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LQ940-04 {ECO:0000313|Proteomes:UP000003217};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000256|ARBA:ARBA00005983}.
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:EHI64872.1}.
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DR EMBL; AEUY02000005; EHI64872.1; -; Genomic_DNA.
DR RefSeq; WP_007893935.1; NZ_AEUY02000005.1.
DR AlphaFoldDB; G5KBX2; -.
DR STRING; 361101.GCA_900102825_01126; -.
DR GeneID; 58554569; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000003217; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHI64872.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHI64872.1}.
FT DOMAIN 1..133
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 303 AA; 33500 MW; 1DE0A17FE1D18EF1 CRC64;
METVYLFVNP FSGKKNEKDL TQHIKESFLQ HGFLEQNITI VTPESASDAF EKAKAASRKG
IDLVIPLGGD GTINKIIGGV HEGGHHTKIG LIPSGTVNNF AKSLSIPLDP DLAIDTILNG
QDKKVDLCKV NEHYMISSLT LGLLADIAAN VTTEEKRKFG PLAFLKDSYR ILKRNRSYYL
TLVDDNGQFA IKTKFLLVTM TNSIAGFPSF SPSATVNDGL LQVYTMKKVS FMKFLLHIND
FRKGDFSMAE EITHFSTKKL SITPSRIKTL ILPRTRIDGD KSDMVPVSLT VLNEAVTVRV
PHS
//
