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Database: UniProt
Entry: A0A1I2MP01_9BACT
LinkDB: A0A1I2MP01_9BACT
Original site: A0A1I2MP01_9BACT 
ID   A0A1I2MP01_9BACT        Unreviewed;       310 AA.
AC   A0A1I2MP01;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Lipid kinase, YegS/Rv2252/BmrU family {ECO:0000313|EMBL:SFF93172.1};
GN   ORFNames=SAMN05216383_102165 {ECO:0000313|EMBL:SFF93172.1};
OS   Prevotella sp. KH2C16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFF93172.1, ECO:0000313|Proteomes:UP000198560};
RN   [1] {ECO:0000313|Proteomes:UP000198560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FOOW01000002; SFF93172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2MP01; -.
DR   STRING; 1855325.SAMN05216383_102165; -.
DR   OrthoDB; 9786026at2; -.
DR   Proteomes; UP000198560; 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: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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFF93172.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        170..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..139
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   310 AA;  35832 MW;  7210BF113B9D5B6C CRC64;
     MAVNENKWGI LYCPKNSFRP QKRWENIEKV LRSERIDFDY VQSESTGSVE RLVKMMINNG
     YRTLIIIGGD SALNDAVNCL MQTEKEVRDQ IALGVIPNGM MNDFAHFWGF QEGEIERSVK
     WLKEHRVRKI DLGRINYKNK HGEPCHRYFL NCINIGLIAT IMNLRRQTRH IVGSRTVSYV
     ISFILMIFQR LEYKMHLKIN GESINRKVMT VCVGNALGYG QTPNAVPYNG LLDVSVVYHP
     EMAQLIEGIY LFVRGKFLNH KSVHPYRTKE VQVRNEEKAL VGIDGRLLNS PLGEYTIRVE
     QEVINFLIPA
//
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