ID A0A1K1Z9T0_STRAR Unreviewed; 273 AA.
AC A0A1K1Z9T0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN02787144_1005242 {ECO:0000313|EMBL:SFX70870.1};
OS Streptomyces atratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1893 {ECO:0000313|EMBL:SFX70870.1, ECO:0000313|Proteomes:UP000181909};
RN [1] {ECO:0000313|EMBL:SFX70870.1, ECO:0000313|Proteomes:UP000181909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK807 {ECO:0000313|EMBL:SFX70870.1,
RC ECO:0000313|Proteomes:UP000181909};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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|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; FPJO01000005; SFX70870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1Z9T0; -.
DR STRING; 1893.SAMN02787144_1005242; -.
DR Proteomes; UP000181909; 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:InterPro.
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 Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
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 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 273 AA; 29084 MW; B4F80C0E8C167988 CRC64;
MPESESEEDT GEDMPLSLRL SIADTLTLGN ATCGFMAVYF TTTGILIPHL TGSDESGMAR
HSAATAVILM LLAAVFDLFD GLVARKLRSS PMGAELDNLS DLISFGLAPA YFVLVYGMVA
DDAHQRVSAL AAIVVLLAVV LRLARFSCVT MKDGMFQGMP SPFGALTVVS IVLLELPFVP
TLLAIVGVAW LMVSRVEYPK PRGVLAVAML SWIVAAMGLL AAWAFDAPGG QLLLQTGCAL
QVVLGAVIPL FATARRVNTF RDNRREARTA QLP
//