ID K8WLK7_9GAMM Unreviewed; 452 AA.
AC K8WLK7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Phosphatidylserine synthase {ECO:0000313|EMBL:EKT61429.1};
DE EC=2.7.8.8 {ECO:0000313|EMBL:EKT61429.1};
GN Name=pssA {ECO:0000313|EMBL:EKT61429.1};
GN ORFNames=OOA_10816 {ECO:0000313|EMBL:EKT61429.1};
OS Providencia burhodogranariea DSM 19968.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT61429.1, ECO:0000313|Proteomes:UP000009336};
RN [1] {ECO:0000313|EMBL:EKT61429.1, ECO:0000313|Proteomes:UP000009336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT61429.1,
RC ECO:0000313|Proteomes:UP000009336};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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:EKT61429.1}.
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DR EMBL; AKKL01000029; EKT61429.1; -; Genomic_DNA.
DR AlphaFoldDB; K8WLK7; -.
DR STRING; 1141662.OOA_10816; -.
DR PATRIC; fig|1141662.3.peg.2194; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_051350_1_0_6; -.
DR Proteomes; UP000009336; 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; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF000850; Phospholipase_D_PSS; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:EKT61429.1}.
FT DOMAIN 134..160
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|SMART:SM00155"
FT DOMAIN 353..380
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|SMART:SM00155"
SQ SEQUENCE 452 AA; 52428 MW; 81563AAE30BB8A28 CRC64;
MMLSKLKQAK HQQYLASIPK LSQSVADVRT LYKTEDFRDA LLEQISIAQH AIYITALYLE
RDDAGKDILH ALYAAKQANP SLEIKILVDW HRAQRGRIGA VANSTNADWY YDVSQQYPEV
DIPVYGIPVN TREALGVLHL KGFIFDDTLL YSGASINDVY LQRHDRYRYD RYQIIKNKQL
TTSMKSYIDD TLLKADAVQL LNTPTRLKTA EFKHIIKQFR LTLRGSSYSF EGNASNSELA
VIPLVGLGKK NDLNRTITHL MGSTENKLTI CTPYFNLPAV LVRIITRLLR EGKQVEIIIG
DKTANDFYIP PEEPFKIIGA LPYLYEINLR RFISRLQKFI DSEQLTIRLW KDGENTYHLK
GMWVDSHWQL ITGNNLNPRA WGLDLENAVL IHDPNQEMQE QRSHELECIR THTIVVSHYR
ELDNIQIYPV KVKKLIRRLR RIRVDRLISR IL
//
