ID   G2IS57_SPHSK            Unreviewed;       265 AA.
AC   G2IS57;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00014944};
DE            EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
GN   Name=pssA {ECO:0000313|EMBL:BAK66217.1};
GN   ORFNames=SLG_15420 {ECO:0000313|EMBL:BAK66217.1};
OS   Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK66217.1, ECO:0000313|Proteomes:UP000001275};
RN   [1] {ECO:0000313|EMBL:BAK66217.1, ECO:0000313|Proteomes:UP000001275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275};
RX   PubMed=22207743; DOI=10.1128/JB.06254-11;
RA   Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA   Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA   Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA   Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT   lignin-derived biaryls and monoaryls.";
RL   J. Bacteriol. 194:534-535(2012).
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 + 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}.
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DR   EMBL; AP012222; BAK66217.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2IS57; -.
DR   STRING; 627192.SLG_15420; -.
DR   KEGG; ssy:SLG_15420; -.
DR   eggNOG; COG1183; Bacteria.
DR   HOGENOM; CLU_049944_1_0_5; -.
DR   OrthoDB; 9777147at2; -.
DR   Proteomes; UP000001275; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:RHEA.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000001275};
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        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          207..242
FT                   /note="CDP-alcohol phosphatidyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08009"
SQ   SEQUENCE   265 AA;  28538 MW;  3AA9BEF75D2D4EE6 CRC64;
     MTPPPRRFAQ RMSSRGITLR QVAPNAVTAM ALCFGLTAIR YGISGDWGRA VAAIIFAGVL
     DGLDGRIARM LHGESRFGAE LDSLSDAIAF GVSPAIILYL WSLQSMPRFG WIVSLVLALS
     CALRLARFNA SIDAAEHPRK AAGFLTGVPA PAGAGLALMP LYAWFITEMD LFRDWRLVGP
     WVVAMALLMI SNLPTLGWKR LRVPPAWRMF ALLLAGVFAA MLMVAPWHAL LALTLGYLAL
     IPAGIISYGR VTRRPAAPGS SPPEG
//