ID D6KN98_9FIRM Unreviewed; 232 AA.
AC D6KN98;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=HMPREF0874_00423 {ECO:0000313|EMBL:EFG25575.2};
OS Veillonella sp. 6_1_27.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=450749 {ECO:0000313|EMBL:EFG25575.2, ECO:0000313|Proteomes:UP000005750};
RN [1] {ECO:0000313|EMBL:EFG25575.2, ECO:0000313|Proteomes:UP000005750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6_1_27 {ECO:0000313|EMBL:EFG25575.2,
RC ECO:0000313|Proteomes:UP000005750};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., McDonald J.,
RA Ambrose C.E., Strauss J.C., Allen-Vercoe E., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Veillonella sp. 6_1_27.";
RL Submitted (MAR-2010) 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 -!- 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; GG770215; EFG25575.2; -; Genomic_DNA.
DR AlphaFoldDB; D6KN98; -.
DR Proteomes; UP000005750; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 232 AA; 24907 MW; 1E346383CCE05469 CRC64;
MILLSGGYDM NKSIIPNLFT SANLAFGVLG ITLSATNNTF CAAICILLSL VADGLDGRVA
RALNVAGPMG RELDSLSDVV GFGVAPAYML YMKELNGLGW IAYVPLLAFA VLGAFRLARF
NIKTDEVHGY FEGLPIPAAG CLAATYVLCG VSVPQFVLVV CMIGIGLLMV SEVKYPDFKG
KSEIYINKLS IVLTAIFVIA CLVYDWHTWA VMIFAGYVMF GLINGALNIV RK
//