ID G5LMP4_SALET Unreviewed; 451 AA.
AC G5LMP4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=O-phosphatidyltransferase {ECO:0000313|EMBL:EHC41055.1};
GN ORFNames=LTSEALA_1828 {ECO:0000313|EMBL:EHC41055.1};
OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC41055.1, ECO:0000313|Proteomes:UP000004642};
RN [1] {ECO:0000313|EMBL:EHC41055.1, ECO:0000313|Proteomes:UP000004642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC41055.1,
RC ECO:0000313|Proteomes:UP000004642};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:EHC41055.1}.
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DR EMBL; AFCJ01000785; EHC41055.1; -; Genomic_DNA.
DR AlphaFoldDB; G5LMP4; -.
DR PATRIC; fig|913241.3.peg.1405; -.
DR Proteomes; UP000004642; 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: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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Transferase {ECO:0000313|EMBL:EHC41055.1}.
FT DOMAIN 133..159
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 352..379
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 451 AA; 52734 MW; 780729B2489C3A1A CRC64;
MLSKFKRNKH QQHLAQLPKI SQSVDDVDFF YTPATFRETL LEKIASATQR ICIVALYLEQ
DDGGKGILDA LYAAKRQRPE LDVRVLVDWH RAQRGRIGAA ASNTNADWYC RLAQENPGID
VPVYGVPINT REALGVLHFK GFIIDDSVLY SGASLNDVYL HQHDKYRYDR YQLIRNRQMA
DIMFDWVTQN LMNGRGVNRL DNTQRPKSPE IKNDIRLYRQ ELRDASYHFQ GDANDEQLSV
TPLVGLGKSS LLNKTIFHLM PCAEHKLTIC TPYFNLPAVL VRNIIQLLRD GKKVEIIVGD
KTANDFYIPE DEPFKIIGAL PYLYEINLRR FLSRLQYYVN TDQLVVRLWK DDDNTYHLKG
MWVDDKWMLL TGNNLNPRAW RLDLENAILI HDPKQELAPQ REKELELIRT HTTIVKHYRD
LQSIADYPIK VRKLIRRLRR IRIDRLISRI L
//
