ID A0A2S8Y860_9PSED Unreviewed; 447 AA.
AC A0A2S8Y860;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Phosphatidylserine synthase {ECO:0000313|EMBL:PRA53741.1};
DE EC=2.7.8.8 {ECO:0000313|EMBL:PRA53741.1};
GN Name=pssA {ECO:0000313|EMBL:PRA53741.1};
GN ORFNames=CQZ98_13815 {ECO:0000313|EMBL:PRA53741.1};
OS Pseudomonas sp. MYb115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA53741.1, ECO:0000313|Proteomes:UP000239970};
RN [1] {ECO:0000313|EMBL:PRA53741.1, ECO:0000313|Proteomes:UP000239970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb115 {ECO:0000313|EMBL:PRA53741.1,
RC ECO:0000313|Proteomes:UP000239970};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000256|ARBA:ARBA00010682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRA53741.1}.
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DR EMBL; PCQM01000008; PRA53741.1; -; Genomic_DNA.
DR RefSeq; WP_027616312.1; NZ_PCQM01000008.1.
DR AlphaFoldDB; A0A2S8Y860; -.
DR Proteomes; UP000239970; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:InterPro.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09134; PLDc_PSS_G_neg_1; 1.
DR CDD; cd09136; PLDc_PSS_G_neg_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586:SF1; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12586; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF000850; Phospholipase_D_PSS; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:PRA53741.1}.
FT DOMAIN 128..154
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 348..375
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 447 AA; 50813 MW; D09842A6FB2E1237 CRC64;
MPLLFKRSLL PKLRSFPLSA DGVSILSGAA EFRRCLLEKI AQATRRIYIV ALYLQQDEAG
QEILDALHAA KAARPELDIV VVVDWLRAQR GLIGAGKQPG NSAWYQQMTR DHASEVPIYG
VPVQTRELFG VLHLKGFVID DSVLYSGASL NNVYLHKFDK YRFDRYHLLH NEALADSMQH
LVQHGLVASK AVHRLDLPNL PTTRSLRNDI GDLRSRLKYA AYDTSQGRVD KTGLSVSPLL
GVGKNNPLNR VICELIASAQ KQLTICTPYF NLPLPITREI NRALARGVKV DIVVGDKTAN
DFYIPPSEPF RVIAALPYLY EISLRRFAKR HQKVIDSGLL NLHLWRDGDN TYHLKGMWVD
ARYTLLTGNN LNPRAFRLDL ENALLIDDPK GELLTPRSAE LTEIFRHTNR IERYQQLESL
VDYPPAVGKF LRRVSRVRIE RLLYRIL
//