ID A0A1H2QPT6_9FLAO Unreviewed; 306 AA.
AC A0A1H2QPT6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Lipid kinase, YegS/Rv2252/BmrU family {ECO:0000313|EMBL:SDW09162.1};
GN ORFNames=SAMN05444411_10155 {ECO:0000313|EMBL:SDW09162.1};
OS Lutibacter oricola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=762486 {ECO:0000313|EMBL:SDW09162.1, ECO:0000313|Proteomes:UP000199595};
RN [1] {ECO:0000313|EMBL:SDW09162.1, ECO:0000313|Proteomes:UP000199595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24956 {ECO:0000313|EMBL:SDW09162.1,
RC ECO:0000313|Proteomes:UP000199595};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNNJ01000001; SDW09162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2QPT6; -.
DR STRING; 762486.SAMN05444411_10155; -.
DR OrthoDB; 9786026at2; -.
DR Proteomes; UP000199595; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; 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:SF54; SPHINGOID LONG-CHAIN BASES KINASE 2, MITOCHONDRIAL; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDW09162.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..136
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 306 AA; 34466 MW; C10B62A20781CCA9 CRC64;
MNLKWFVIVN PTSGNGISKK LWPKIKQELI AQQFNFEVAF TEHEEHSTEL VQNAINNNFL
KIISVGGDGS LHNIINGIFN SNITNYKSIK LGVIPIGTGN DWVKSYQIPI NYKKAIEIIK
EEYIYQQDIG KLSLTTLKKD FYFNNLAGIG FDGHVVNKVH KYKYLGFLAY IIGALVSLIG
FKRKNLHIEF NETTISGKSL MLLIGIGKYS GGGMQLTENV KTNDGLFDIS YVKKVSFFTV
IKHISKIFNG KATQLPIFNT YKTSVIKVSI KNNENIYIQA DGELIETDNF TASIIPRALQ
FIVPKL
//
