ID K5E138_RHOBT Unreviewed; 316 AA.
AC K5E138;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00017171};
DE EC=2.7.8.8 {ECO:0000256|ARBA:ARBA00013174};
DE AltName: Full=Phosphatidylserine synthase {ECO:0000256|ARBA:ARBA00032361};
GN ORFNames=RBSH_05225 {ECO:0000313|EMBL:EKJ99470.1};
OS Rhodopirellula baltica SH28.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993517 {ECO:0000313|EMBL:EKJ99470.1, ECO:0000313|Proteomes:UP000007993};
RN [1] {ECO:0000313|EMBL:EKJ99470.1, ECO:0000313|Proteomes:UP000007993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH28 {ECO:0000313|EMBL:EKJ99470.1,
RC ECO:0000313|Proteomes:UP000007993};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKJ99470.1}.
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DR EMBL; AMCW01000145; EKJ99470.1; -; Genomic_DNA.
DR RefSeq; WP_007334612.1; NZ_AMCW01000145.1.
DR AlphaFoldDB; K5E138; -.
DR PATRIC; fig|993517.3.peg.5657; -.
DR Proteomes; UP000007993; 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; 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; 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 49..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 34273 MW; 3B8112F52CEB0414 CRC64;
MIEMSELKPR LPIQDDDSVD DESDLIQEDG VTERSKFGRR RRRGKKRRLT LAVLPTLLTL
GNGVCGLAAI AIAVSTESLD WTPESKLFAA GLLIFGGMLF DALDGSAARL TGQASRFGAE
LDSLCDAVTF GVAPAVIVWR ISDVLLQRLT WGIGVLFALC VLIRLARFNV ETPEDDDHEG
FEGLPSPAAA GTIAAFAIAI PDLADFSVGE AYPEWIHSMA GLALDASHYV IPTLALVLAF
LMVSRYEYPH VFAQLVRGRR APHQIGQALF AVVGLFLLHW VALPVVFCYF AFMSPIRSLL
QRNSKPATST SSVEGG
//
