ID Q9FDI8_RHIML Unreviewed; 289 AA.
AC Q9FDI8;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 127.
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 EC=2.7.8.8 {ECO:0000256|ARBA:ARBA00013174};
DE AltName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00017171};
DE AltName: Full=Phosphatidylserine synthase {ECO:0000256|ARBA:ARBA00032361};
GN Name=pss {ECO:0000313|EMBL:AAG00422.1};
GN Synonyms=pssA {ECO:0000313|EMBL:MQW83196.1};
GN ORFNames=GHK55_26630 {ECO:0000313|EMBL:MQW83196.1};
OS Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=382 {ECO:0000313|EMBL:AAG00422.1};
RN [1] {ECO:0000313|EMBL:AAG00422.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=14996797; DOI=10.1128/JB.186.6.1667-1677.2004;
RA Sohlenkamp C., de Rudder K.E., Geiger O.;
RT "Phosphatidylethanolamine is not essential for growth of Sinorhizobium
RT meliloti on complex culture media.";
RL J. Bacteriol. 186:1667-1677(2004).
RN [2] {ECO:0000313|EMBL:MQW83196.1, ECO:0000313|Proteomes:UP000483613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA1002 {ECO:0000313|EMBL:MQW83196.1,
RC ECO:0000313|Proteomes:UP000483613};
RX PubMed=23425606;
RA Sugawara M., Epstein B., Badgley B.D., Unno T., Xu L., Reese J.,
RA Gyaneshwar P., Denny R., Mudge J., Bharti A.K., Farmer A.D., May G.D.,
RA Woodward J.E., Medigue C., Vallenet D., Lajus A., Rouy Z., Martinez-Vaz B.,
RA Tiffin P., Young N.D., Sadowsky M.J.;
RT "Comparative genomics of the core and accessory genomes of 48 Sinorhizobium
RT strains comprising five genospecies.";
RL Genome Biol. 14:0-R17(2013).
RN [3] {ECO:0000313|EMBL:MQW83196.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA1002 {ECO:0000313|EMBL:MQW83196.1};
RA Sugawara M., Epstein B., Badgley B., Unno T., Xu L., Reese J.,
RA Gyaneshwar P., Denny R., Mudege J., Bharti A., Farmer A., May G.,
RA Woodward J., Medigue C., Vallenet D., Lajus A., Rouy Z., Martinez-Vaz B.,
RA Tiffin P., Young N., Sadowsky M.;
RL Submitted (OCT-2019) 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 + L-serine = a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000287};
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; AF247564; AAG00422.1; -; Genomic_DNA.
DR EMBL; WISX01000249; MQW83196.1; -; Genomic_DNA.
DR RefSeq; WP_010969056.1; NZ_WISY01000138.1.
DR STRING; 382.DU99_05820; -.
DR GeneID; 61602581; -.
DR KEGG; smer:DU99_05820; -.
DR PATRIC; fig|382.52.peg.1188; -.
DR OMA; IFFDFFD; -.
DR Proteomes; UP000483613; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR012616; CDP-OH_P_trans_C.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR NCBIfam; TIGR00473; pssA; 1.
DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR Pfam; PF08009; CDP-OH_P_tran_2; 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 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..262
FT /note="CDP-alcohol phosphatidyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08009"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 31483 MW; 6F05D3BBA0D032E3 CRC64;
MEEPRHEQSA GIPEAAEHVG ATGTHDKARG PRLREIPLRL MVPNMITVLA ICAGLSGVRL
AFENRFELAV AMVLLAAFLD GIDGRIARLL KATSSFGVQM DSLADIINFG VAPALVLYVF
LLDQARSLGW IAALIYAIAV GLRLARFNVM AERQVKASWQ SEYFVGVPAP AGAMLVLLPV
YLGLLGLAPE RTFALIASVY TVLIAFLMVS RLPVWSGKSE NRVRRDLVLP VILVVVFYVA
TLMTYTWETM VVTAVAYLVS LPFGARSWQR KYGDWPGGHG NDGLPGDSE
//
