ID C6XF98_LIBAP Unreviewed; 298 AA.
AC C6XF98;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00014944};
DE EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
GN Name=pssA {ECO:0000313|EMBL:ACT57051.1};
GN OrderedLocusNames=CLIBASIA_02325 {ECO:0000313|EMBL:ACT57051.1};
OS Liberibacter asiaticus (strain psy62).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT57051.1, ECO:0000313|Proteomes:UP000002744};
RN [1] {ECO:0000313|EMBL:ACT57051.1, ECO:0000313|Proteomes:UP000002744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX PubMed=19589076; DOI=10.1094/MPMI-22-8-1011;
RA Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA Gottwald T.;
RT "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus
RT Liberibacter asiaticus' obtained through metagenomics.";
RL Mol. Plant Microbe Interact. 22:1011-1020(2009).
RN [2] {ECO:0000313|EMBL:ACT57051.1, ECO:0000313|Proteomes:UP000002744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX PubMed=21784907; DOI=10.1128/AEM.05111-11;
RA Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H., Duan Y.;
RT "Diversity and plasticity of the intracellular plant pathogen and insect
RT symbiont, 'Candidatus Liberibacter asiaticus', revealed by hyper variable
RT prophage genes with intragenic tandem repeats.";
RL Appl. Environ. Microbiol. 77:6663-6673(2011).
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}.
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DR EMBL; CP001677; ACT57051.1; -; Genomic_DNA.
DR AlphaFoldDB; C6XF98; -.
DR STRING; 537021.CLIBASIA_02325; -.
DR KEGG; las:CLIBASIA_02325; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_049944_1_0_5; -.
DR OrthoDB; 9777147at2; -.
DR Proteomes; UP000002744; 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 55..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 298 AA; 33886 MW; A8AD94CC92A0EACB CRC64;
MGNTLQCKEI PRGKKKYNVL PDDFVVPSDQ DEARYSFYKG KRWSLQEKEI PPFKFLFPNL
VTILAICAGF SGIGSAIEGN YETAVCMVLV AAFLDGIDGR IARFMEATSK FGAQLDSLAD
VINFGVAPSL VTYIAVLRQA HAFGWSIALM YTIAISLRLA RFNIMNDCDE KDNWKSEYFV
GVPAPLGAIL LMLPLYINFL GFKISVIYGY GSTIYAMIIS FLLCSRLPVW SGKKIHRKFV
LPIVLCSVAY IAFMIHFLWE MIIFSTLCYI MLLPISFYCW KKRYGIKPEQ KKHKDYIK
//
