PSS_ECOLI
ID PSS_ECOLI Reviewed; 451 AA.
AC P23830; P78100; P78256;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase;
DE EC=2.7.8.8;
DE AltName: Full=Phosphatidylserine synthase;
GN Name=pssA; Synonyms=pss; OrderedLocusNames=b2585, JW2569;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RX PubMed=2002065; DOI=10.1016/s0021-9258(19)67791-4;
RA Dechavigny A., Heacock P.N., Dowhan W.;
RT "Sequence and inactivation of the pss gene of Escherichia coli.
RT Phosphatidylethanolamine may not be essential for cell viability.";
RL J. Biol. Chem. 266:5323-5332(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP REVIEW.
RX PubMed=1323044; DOI=10.1016/0076-6879(92)09036-3;
RA Dowhan W.;
RT "Phosphatidylserine synthase from Escherichia coli.";
RL Methods Enzymol. 209:287-298(1992).
RN [6]
RP INTERACTION WITH ACP; YBGC AND PLSB.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16294310; DOI=10.1002/pmic.200500115;
RA Gully D., Bouveret E.;
RT "A protein network for phospholipid synthesis uncovered by a variant of the
RT tandem affinity purification method in Escherichia coli.";
RL Proteomics 6:282-293(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC -!- SUBUNIT: Multimeric. Interacts with ACP, YbgC and PlsB, forming
CC altogether a complex at the inner membrane.
CC {ECO:0000269|PubMed:16294310}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
CC membrane protein; Cytoplasmic side.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000305}.
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DR EMBL; M58699; AAA97504.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75638.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16470.2; -; Genomic_DNA.
DR RefSeq; NP_417080.4; NC_000913.3.
DR RefSeq; WP_000949265.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P23830; -.
DR SMR; P23830; -.
DR BioGRID; 4259429; 210.
DR DIP; DIP-10593N; -.
DR IntAct; P23830; 35.
DR STRING; 511145.b2585; -.
DR jPOST; P23830; -.
DR PaxDb; P23830; -.
DR PRIDE; P23830; -.
DR EnsemblBacteria; AAC75638; AAC75638; b2585.
DR EnsemblBacteria; BAA16470; BAA16470; BAA16470.
DR GeneID; 66673525; -.
DR GeneID; 947059; -.
DR KEGG; ecj:JW2569; -.
DR KEGG; eco:b2585; -.
DR PATRIC; fig|1411691.4.peg.4149; -.
DR EchoBASE; EB0774; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_051350_1_0_6; -.
DR InParanoid; P23830; -.
DR OMA; YLSTLYI; -.
DR PhylomeDB; P23830; -.
DR BioCyc; EcoCyc:PHOSPHASERSYN-MON; -.
DR BioCyc; MetaCyc:PHOSPHASERSYN-MON; -.
DR BRENDA; 2.7.8.8; 2026.
DR PRO; PR:P23830; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IDA:EcoCyc.
DR GO; GO:0005543; F:phospholipid binding; IDA:EcoCyc.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:EcoCyc.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586; PTHR12586; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..451
FT /note="CDP-diacylglycerol--serine O-
FT phosphatidyltransferase"
FT /id="PRO_0000056824"
FT DOMAIN 133..159
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 352..379
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 119..154
FT /note="Hydrophobic"
FT REGION 239..284
FT /note="Hydrophobic"
FT CONFLICT 32
FT /note="A -> R (in Ref. 1; AAA97504)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="R -> DD (in Ref. 1; AAA97504)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..167
FT /note="KYR -> NIA (in Ref. 1; AAA97504)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="LL -> FV (in Ref. 1; AAA97504)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="P -> S (in Ref. 1; AAA97504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 52802 MW; 9E9A2A5C4B4C814F CRC64;
MLSKFKRNKH QQHLAQLPKI SQSVDDVDFF YAPADFRETL LEKIASAKQR ICIVALYLEQ
DDGGKGILNA LYEAKRQRPE LDVRVLVDWH RAQRGRIGAA ASNTNADWYC RMAQENPGVD
VPVYGVPINT REALGVLHFK GFIIDDSVLY SGASLNDVYL HQHDKYRYDR YHLIRNRKMS
DIMFEWVTQN IMNGRGVNRL DDVNRPKSPE IKNDIRLFRQ ELRDAAYHFQ GDADNDQLSV
TPLVGLGKSS LLNKTIFHLM PCAEQKLTIC TPYFNLPAIL VRNIIQLLRE GKKVEIIVGD
KTANDFYIPE DEPFKIIGAL PYLYEINLRR FLSRLQYYVN TDQLVVRLWK DDDNTYHLKG
MWVDDKWMLI TGNNLNPRAW RLDLENAILI HDPQLELAPQ REKELELIRE HTTIVKHYRD
LQSIADYPVK VRKLIRRLRR IRIDRLISRI L
