ID D2TU41_CITRI Unreviewed; 451 AA.
AC D2TU41;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=CDP-diacylglycerol-serine O-phosphatidyltransferase {ECO:0000313|EMBL:CBG89273.1};
DE EC=2.7.8.8 {ECO:0000313|EMBL:CBG89273.1};
GN Name=pssA {ECO:0000313|EMBL:CBG89273.1};
GN OrderedLocusNames=ROD_25301 {ECO:0000313|EMBL:CBG89273.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89273.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG89273.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG89273.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000256|ARBA:ARBA00010682}.
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DR EMBL; FN543502; CBG89273.1; -; Genomic_DNA.
DR RefSeq; WP_012906707.1; NC_013716.1.
DR AlphaFoldDB; D2TU41; -.
DR STRING; 637910.ROD_25301; -.
DR KEGG; cro:ROD_25301; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_051350_1_0_6; -.
DR OrthoDB; 8543662at2; -.
DR Proteomes; UP000001889; 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: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:CBG89273.1}.
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; 52742 MW; 8268332412D10D37 CRC64;
MLSKFKRNKH QQHLAQLPKI SQSVADVNFF YAPADFREAL LEKIASAKRR ICIVALYLEQ
DDGGKGVLDA LYEAKRQRPE LDVRVLVDWH RAQRGRIGAA ASNTNADWYC RMAQENPGVD
VPVYGVPINT REALGVLHFK GFIIDDSVLY SGASLNDVYL HQHDKYRYDR YHLIRNARMS
DIMFEWVNQN LMHGRGVNRL DDTQRPKSPE IKNDIRLYRQ ELRDAAYHFQ GDADNEQLSV
TPLVGLGKSS QLNKTIFHLM PCAEQKLTIC TPYFNLPAIL VRNIIQLLRE GKKVEIIVGD
KTANDFYIPE NEPFKIIGAL PYLYEINLRR FLSRLQYYVN TDQLIVRLWK DEDNSYHLKG
MWVDDNWMLL TGNNLNPRAW RLDLENAILI HDPKQELAAQ REKELELIRT HTTIVKHYRD
LQSIADYPVK VRKLIRRLRR IRIDRLISRI L
//
