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Entry: A0A160F2S2_9BACI
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ID   A0A160F2S2_9BACI        Unreviewed;       179 AA.
AC   A0A160F2S2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   Name=pssA {ECO:0000313|EMBL:ANB60559.1};
GN   ORFNames=GFC30_2725 {ECO:0000313|EMBL:ANB60559.1};
OS   Anoxybacillus amylolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB60559.1, ECO:0000313|Proteomes:UP000076865};
RN   [1] {ECO:0000313|EMBL:ANB60559.1, ECO:0000313|Proteomes:UP000076865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB60559.1,
RC   ECO:0000313|Proteomes:UP000076865};
RX   PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA   Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA   Gambacorta A., Nicolaus B.;
RT   "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT   bacterium isolated from Mount Rittmann (Antarctica).";
RL   Syst. Appl. Microbiol. 29:300-307(2006).
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; CP015438; ANB60559.1; -; Genomic_DNA.
DR   RefSeq; WP_066326299.1; NZ_CP015438.1.
DR   AlphaFoldDB; A0A160F2S2; -.
DR   KEGG; aamy:GFC30_2725; -.
DR   PATRIC; fig|294699.3.peg.2806; -.
DR   OrthoDB; 9777147at2; -.
DR   Proteomes; UP000076865; 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: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   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:UP000076865};
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        101..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   179 AA;  19825 MW;  C577CEEF1931EC3C CRC64;
     MFLSDYIDHT LKKLKANTAN ILTLTNLTLG GFSILFTLKG QLNASLLFIF LAALADRFDG
     TVARKLGIES ELGKQLDSMS DIISFGVAPA LLLYQSLMQD FGVPGAFFTI LYIGCGAFRL
     ARFNITENNG YFCGLPITAA GVLLTFSYFG VHYFPPQFFF FLMMTLSFLM VGTFKLKKV
//
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