ID A8SK01_9FIRM Unreviewed; 292 AA.
AC A8SK01;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Lipid kinase, YegS/Rv2252/BmrU family {ECO:0000313|EMBL:EDP23959.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:EDP23959.1};
GN ORFNames=PEPMIC_00538 {ECO:0000313|EMBL:EDP23959.1};
OS Parvimonas micra ATCC 33270.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Parvimonas.
OX NCBI_TaxID=411465 {ECO:0000313|EMBL:EDP23959.1, ECO:0000313|Proteomes:UP000003162};
RN [1] {ECO:0000313|EMBL:EDP23959.1, ECO:0000313|Proteomes:UP000003162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33270 {ECO:0000313|EMBL:EDP23959.1,
RC ECO:0000313|Proteomes:UP000003162};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Peptostreptococcus micros (ATCC 33270).";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDP23959.1, ECO:0000313|Proteomes:UP000003162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33270 {ECO:0000313|EMBL:EDP23959.1,
RC ECO:0000313|Proteomes:UP000003162};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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:EDP23959.1}.
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DR EMBL; ABEE02000016; EDP23959.1; -; Genomic_DNA.
DR AlphaFoldDB; A8SK01; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_0_9; -.
DR Proteomes; UP000003162; 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 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:EDP23959.1};
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:EDP23959.1}.
FT DOMAIN 1..131
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 292 AA; 32655 MW; C8B89B098B8E42B9 CRC64;
MRKLMFILNP NASGFKKFDF KDAIENYLKD KNLDFNYDIK CSTKEGESVF IAENAVKDGF
NELIAVGGDG TINEVGDVAI KNNLKLGVIP AGTGNDYMNS LNESCNFIIC MEKIIRGNTI
FIDYGSFADK SFFNVACVGF GAEVNIYAHK VKKLIPSGLA YKIAIALALF GHKRKRYKII
VDNVEYEDDY FLIAIGIGSK FGGKLNLLPS ADMQDGLLDI CAIKYKSKFD IIKKIKTIVN
ATHVNEDITS YFKAKKIKII SENIEINFDG EDMSCDDEVE FIVNDKKVEL IM
//
