ID B4SMQ8_STRM5 Unreviewed; 204 AA.
AC B4SMQ8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00014944};
DE EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
DE Flags: Precursor;
GN OrderedLocusNames=Smal_2417 {ECO:0000313|EMBL:ACF52120.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF52120.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF52120.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF52120.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC the acidic phospholipids. {ECO:0000256|ARBA:ARBA00003973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001566};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005042}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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; CP001111; ACF52120.1; -; Genomic_DNA.
DR RefSeq; WP_012511419.1; NC_011071.1.
DR AlphaFoldDB; B4SMQ8; -.
DR STRING; 391008.Smal_2417; -.
DR KEGG; smt:Smal_2417; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_049944_5_2_6; -.
DR OrthoDB; 9777147at2; -.
DR Proteomes; UP000001867; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 204 AA; 22332 MW; EF43E86636B13189 CRC64;
MKRHFSMLRE FQLADWFTLA NAFCGTGAVF AAMRFLQDGE RGYLLFGMAL IPLAFIFDAL
DGHIARWRKS SSTLGRELDS LSDVISFGVA PAALAYACGM QGGWDWLVLS YFVCCGVSRL
ARYNVTAEAL AGDEGKVKYF EGTPIPTSLL LVIVLAIAAG TGAIGQDIWF GQWQIGPWQL
HPMVLLFALS GSLMISKTLR IPKP
//
