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Database: UniProt
Entry: D8MVX9_ERWBE
LinkDB: D8MVX9_ERWBE
Original site: D8MVX9_ERWBE 
ID   D8MVX9_ERWBE            Unreviewed;       451 AA.
AC   D8MVX9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Phosphatidylserine synthase (CDP-diacylglycerol-serine O-phosphatidyltransferase) {ECO:0000313|EMBL:CAX60986.1};
GN   Name=pssA {ECO:0000313|EMBL:CAX60986.1};
GN   OrderedLocusNames=EbC_34550 {ECO:0000313|EMBL:CAX60986.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX60986.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX60986.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC       family. {ECO:0000256|ARBA:ARBA00010682}.
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DR   EMBL; FP236843; CAX60986.1; -; Genomic_DNA.
DR   RefSeq; WP_013203471.1; NC_014306.1.
DR   AlphaFoldDB; D8MVX9; -.
DR   STRING; 634500.EbC_34550; -.
DR   KEGG; ebi:EbC_34550; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_051350_1_0_6; -.
DR   Proteomes; UP000008793; Chromosome.
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: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; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW   Transferase {ECO:0000313|EMBL:CAX60986.1}.
FT   DOMAIN          352..379
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   451 AA;  52625 MW;  BC01C98B2EF0663E CRC64;
     MLSKFKRNKH QQHLAQLPKL SQSAADFTTL YSAADFRKTL LEKIAGAKHR ICIVALYLEN
     DDGGRSILNA LYEAKRLRPE LDVRVLVDWH RAQRGRIGAA RTATNADWYC ELADAHPDIH
     ITVYGVPVNT REALGVLHLK GSIIDDTLFY TGASLNDVYL HQHDKYRYDR YQLITNPTLA
     NTMFDWIETN LIQAEAVHRL DQHERPKSPE IKNETRQFRQ DLRGFDYEFE GDANNEQLAV
     TPLVGLGKRS LLNKTIFHLM PCAEQKLTLC TPYFNMPAIL VRNIIWLLRQ GREVEIIVGD
     KTANDFYIPE DQPFKIIGAL PYLYEINLRR FLSRLQYYVT NGQLTVRLWK DGENSYHLKG
     MWVDDEWLLI TGNNLNPRAW RLDLENAVLI HDPLQQLVEQ SRHELALIRQ NTTVVEHFRD
     LESIADYPLK VRKLIRRLRR IRIDRLISRI L
//
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