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Database: UniProt
Entry: V2Q0P1_9BACT
LinkDB: V2Q0P1_9BACT
Original site: V2Q0P1_9BACT 
ID   V2Q0P1_9BACT            Unreviewed;       264 AA.
AC   V2Q0P1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, 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=N508_001297 {ECO:0000313|EMBL:USF24214.1}, N508_00758
GN   {ECO:0000313|EMBL:ESJ98542.1};
OS   Mucispirillum schaedleri ASF457.
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Mucispirillaceae; Mucispirillum.
OX   NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ98542.1};
RN   [1] {ECO:0000313|EMBL:ESJ98542.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF457 {ECO:0000313|EMBL:ESJ98542.1};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
RN   [2] {ECO:0000313|EMBL:USF24214.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASF457 {ECO:0000313|EMBL:USF24214.1};
RA   Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL   Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:USF24214.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASF457 {ECO:0000313|EMBL:USF24214.1};
RA   Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA   Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT   "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT   Model to Study Microbiome Function.";
RL   Submitted (JUN-2022) 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|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR   EMBL; AYGZ01000012; ESJ98542.1; -; Genomic_DNA.
DR   EMBL; CP097562; USF24214.1; -; Genomic_DNA.
DR   AlphaFoldDB; V2Q0P1; -.
DR   STRING; 1379858.N508_00758; -.
DR   PATRIC; fig|1379858.3.peg.751; -.
DR   eggNOG; COG1183; Bacteria.
DR   HOGENOM; CLU_049944_3_0_0; -.
DR   Proteomes; UP000017429; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000017429};
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        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   264 AA;  29314 MW;  C1A9339C08217BAB CRC64;
     MSMFSEKSGK LNMTLRNRNI ILPNFITIMG LLCGIYSIML SVGSRIVEGD NFVYSAYFLL
     LAAFFDGIDG KVARIVNGTS DFGVQLDSLC DMVSFGVAPA ILVYEWLLKG FDRLGIVAVF
     LFVACGALRL ARFNVQSSKI SNVFFVGLPI PAAAAFIATS VLFIHKLGFD LEKAALSMFF
     LASIYLLAFL MVSTVPFYSF KKISYFKARP FQALIVMVVF ISILVLYFEV VSFVMISVYI
     TLGLLLACYK LIKGKQKTAE RNQQ
//
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