YEGS_SALTY
ID YEGS_SALTY Reviewed; 299 AA.
AC Q8ZNP1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable lipid kinase YegS;
DE EC=2.7.1.-;
GN Name=yegS; OrderedLocusNames=STM2140;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), FUNCTION, COFACTOR, SUBUNIT, AND
RP POSSIBLE INTERACTION WITH SKP.
RC STRAIN=SL3261;
RX PubMed=17393457; DOI=10.1002/prot.21386;
RA Nichols C.E., Lamb H.K., Lockyer M., Charles I.G., Pyne S., Hawkins A.R.,
RA Stammers D.K.;
RT "Characterization of Salmonella typhimurium yegS, a putative lipid kinase
RT homologous to eukaryotic sphingosine and diacylglycerol kinases.";
RL Proteins 68:13-25(2007).
CC -!- FUNCTION: In vitro does not phosphorylate diacylglycerol, sphingosine,
CC N,N-dimethylsphingosine; threo-dihydrosphingosine, erythro-
CC dihydrosphingosine, C2 ceramide, C6 ceramide, phosphatidylinositol or
CC dimethylsphingosine. The potential in vivo substrate is unknown.
CC {ECO:0000269|PubMed:17393457}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17393457, ECO:0000305};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17393457, ECO:0000305};
CC Note=Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute.
CC 2 Ca(2+) ions are seen in the crystal structure; one of the two
CC occupies the same site as Mg(2+) in other family members.
CC {ECO:0000269|PubMed:17393457, ECO:0000305};
CC -!- SUBUNIT: Homodimer. May interact with the periplasmic chaperone Skp
CC (also known as OmpH); this suggests the protein may be translocated to
CC the periplasm and then sorted to the outer membrane.
CC {ECO:0000269|PubMed:17393457}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS
CC lipid kinase subfamily. {ECO:0000305}.
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DR EMBL; AE006468; AAL21043.1; -; Genomic_DNA.
DR RefSeq; NP_461084.1; NC_003197.2.
DR RefSeq; WP_001273389.1; NC_003197.2.
DR PDB; 2P1R; X-ray; 2.50 A; A/B/C/D=1-299.
DR PDBsum; 2P1R; -.
DR AlphaFoldDB; Q8ZNP1; -.
DR SMR; Q8ZNP1; -.
DR STRING; 99287.STM2140; -.
DR PaxDb; Q8ZNP1; -.
DR EnsemblBacteria; AAL21043; AAL21043; STM2140.
DR GeneID; 1253661; -.
DR KEGG; stm:STM2140; -.
DR PATRIC; fig|99287.12.peg.2265; -.
DR HOGENOM; CLU_045532_1_1_6; -.
DR OMA; GFDSRVN; -.
DR PhylomeDB; Q8ZNP1; -.
DR BioCyc; SENT99287:STM2140-MON; -.
DR EvolutionaryTrace; Q8ZNP1; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001727; F:lipid kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10330; -; 1.
DR HAMAP; MF_01377; YegS; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR022433; Lip_kinase_YegS.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR TIGRFAMs; TIGR03702; lip_kinase_YegS; 1.
DR TIGRFAMs; TIGR00147; TIGR00147; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..299
FT /note="Probable lipid kinase YegS"
FT /id="PRO_0000292157"
FT DOMAIN 2..133
FT /note="DAGKc"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 66..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2P1R"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 187..204
FT /evidence="ECO:0007829|PDB:2P1R"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:2P1R"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 248..268
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 271..282
FT /evidence="ECO:0007829|PDB:2P1R"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:2P1R"
SQ SEQUENCE 299 AA; 32029 MW; 4026FEFD5F2F0197 CRC64;
MANFPASLLI LNGKSADNQP LREAITLLRD EGIQIHVRVT WEKGDAQRYV DEARRLGVET
VIAGGGDGTI NEVSTALIQI RDGVAPALGL LPLGTANDFA TSAGIPEALD KALKLAIAGN
AMEIDMAMVN DKTCFINMAT GGFGTRITTE TPEKLKAALG GVSYLIHGLM RMDTLTPDRC
EIRGENFHWQ GDALVIGIGN GRQAGGGQQL CPTALINDGL LQLRIFTGEE LLPALFSTLT
QSDDNPNIID GASAWFDIHA PHEITFNLDG EPLSGQEFHI EVLPGALRCR LPPDCPLLR
