PLSB_ECOLI
ID PLSB_ECOLI Reviewed; 807 AA.
AC P0A7A7; P00482; Q2M6R3; Q9S683;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glycerol-3-phosphate acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.15 {ECO:0000269|PubMed:10231527};
GN Name=plsB; OrderedLocusNames=b4041, JW4001;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6309817; DOI=10.1016/s0021-9258(17)44354-7;
RA Lightner V.A., Bell R.M., Modrich P.;
RT "The DNA sequences encoding plsB and dgk loci of Escherichia coli.";
RL J. Biol. Chem. 258:10856-10861(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ALA-349.
RC STRAIN=K12;
RX PubMed=10074094; DOI=10.1128/jb.181.6.1944-1946.1999;
RA Heath R.J., Rock C.O.;
RT "A missense mutation accounts for the defect in the glycerol-3-phosphate
RT acyltransferase expressed in the plsB26 mutant.";
RL J. Bacteriol. 181:1944-1946(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 781-807.
RC STRAIN=K12;
RX PubMed=1644758; DOI=10.1128/jb.174.16.5309-5316.1992;
RA Nichols B.P., Green J.M.;
RT "Cloning and sequencing of Escherichia coli ubiC and purification of
RT chorismate lyase.";
RL J. Bacteriol. 174:5309-5316(1992).
RN [7]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=6350296; DOI=10.1016/s0021-9258(17)44355-9;
RA Green P.R., Vanaman T.C., Modrich P., Bell R.M.;
RT "Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide
RT analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase.";
RL J. Biol. Chem. 258:10862-10866(1983).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=4943977; DOI=10.1016/0005-2736(71)90145-3;
RA White D.A., Albright F.R., Lennarz W.J., Schnaitman C.A.;
RT "Distribution of phospholipid-synthesizing enzymes in the wall and membrane
RT subfractions of the envelope of Escherichia coli.";
RL Biochim. Biophys. Acta 249:636-642(1971).
RN [9]
RP IDENTIFICATION.
RC STRAIN=K12;
RX PubMed=6251087; DOI=10.1016/s0021-9258(19)70578-x;
RA Lightner V.A., Larson T.J., Tailleur P., Kantor G.D., Raetz C.R.,
RA Bell R.M., Modrich P.;
RT "Membrane phospholipid synthesis in Escherichia coli. Cloning of a
RT structural gene (plsB) of the sn-glycerol-3-phosphate acyl/transferase.";
RL J. Biol. Chem. 255:9413-9420(1980).
RN [10]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=6997313; DOI=10.1016/s0021-9258(19)70579-1;
RA Larson T.J., Lightner V.A., Green P.R., Modrich P., Bell R.M.;
RT "Membrane phospholipid synthesis in Escherichia coli. Identification of the
RT sn-glycerol-3-phosphate acyltransferase polypeptide as the plsB gene
RT product.";
RL J. Biol. Chem. 255:9421-9426(1980).
RN [11]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FATTY ACYL DONOR SPECIFICITY.
RX PubMed=7026564; DOI=10.1016/s0021-9258(19)68570-4;
RA Green P.R., Merrill A.H. Jr., Bell R.M.;
RT "Membrane phospholipid synthesis in Escherichia coli. Purification,
RT reconstitution, and characterization of sn-glycerol-3-phosphate
RT acyltransferase.";
RL J. Biol. Chem. 256:11151-11159(1981).
RN [12]
RP MUTAGENESIS OF HIS-306 AND ASP-311.
RC STRAIN=K12;
RX PubMed=9515909; DOI=10.1128/jb.180.6.1425-1430.1998;
RA Heath R.J., Rock C.O.;
RT "A conserved histidine is essential for glycerolipid acyltransferase
RT catalysis.";
RL J. Bacteriol. 180:1425-1430(1998).
RN [13]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP HIS-306; SER-308; ASP-311; PHE-351; ILE-352; ARG-354; GLU-385; GLY-386;
RP SER-389 AND PRO-421.
RC STRAIN=K12;
RX PubMed=10231527; DOI=10.1021/bi982805d;
RA Lewin T.M., Wang P., Coleman R.A.;
RT "Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate
RT acyltransferase reaction.";
RL Biochemistry 38:5764-5771(1999).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ACP; YBGC AND PSSA.
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).
RN [15]
RP FUNCTION IN PHOSPHOLIPID BIOSYNTHESIS.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17645809; DOI=10.1186/1471-2180-7-69;
RA Yoshimura M., Oshima T., Ogasawara N.;
RT "Involvement of the YneS/YgiH and PlsX proteins in phospholipid
RT biosynthesis in both Bacillus subtilis and Escherichia coli.";
RL BMC Microbiol. 7:69-69(2007).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to
CC glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This
CC enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor.
CC {ECO:0000269|PubMed:17645809, ECO:0000269|PubMed:6997313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:10231527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:10231527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000269|PubMed:10231527};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=49 uM for glycerol-3-phosphate {ECO:0000269|PubMed:10231527,
CC ECO:0000269|PubMed:7026564};
CC Vmax=13.1 nmol/min/mg enzyme with glycerol-3-phosphate as substrate
CC {ECO:0000269|PubMed:10231527, ECO:0000269|PubMed:7026564};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:10231527,
CC ECO:0000269|PubMed:7026564};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBUNIT: Interacts with ACP, YbgC and PssA, forming altogether a
CC complex at the inner membrane. {ECO:0000269|PubMed:16294310}.
CC -!- INTERACTION:
CC P0A7A7; P0A6A8: acpP; NbExp=4; IntAct=EBI-542961, EBI-542566;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16294310,
CC ECO:0000269|PubMed:4943977}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16294310, ECO:0000269|PubMed:4943977}; Cytoplasmic
CC side {ECO:0000269|PubMed:16294310, ECO:0000269|PubMed:4943977}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43135.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; K00127; AAA24395.1; -; Genomic_DNA.
DR EMBL; AF106625; AAD20588.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43135.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77011.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78043.1; -; Genomic_DNA.
DR EMBL; M93413; AAA24718.1; -; Genomic_DNA.
DR EMBL; M93136; AAA24713.1; -; Genomic_DNA.
DR PIR; A00565; XUECAG.
DR RefSeq; NP_418465.4; NC_000913.3.
DR RefSeq; WP_000017354.1; NZ_STEB01000022.1.
DR AlphaFoldDB; P0A7A7; -.
DR SMR; P0A7A7; -.
DR BioGRID; 4261720; 246.
DR BioGRID; 852835; 1.
DR DIP; DIP-29380N; -.
DR IntAct; P0A7A7; 37.
DR STRING; 511145.b4041; -.
DR SwissLipids; SLP:000001804; -.
DR jPOST; P0A7A7; -.
DR PaxDb; P0A7A7; -.
DR PRIDE; P0A7A7; -.
DR EnsemblBacteria; AAC77011; AAC77011; b4041.
DR EnsemblBacteria; BAE78043; BAE78043; BAE78043.
DR GeneID; 66672044; -.
DR GeneID; 948541; -.
DR KEGG; ecj:JW4001; -.
DR KEGG; eco:b4041; -.
DR PATRIC; fig|511145.12.peg.4158; -.
DR EchoBASE; EB0733; -.
DR eggNOG; COG2937; Bacteria.
DR HOGENOM; CLU_015407_0_0_6; -.
DR InParanoid; P0A7A7; -.
DR OMA; EVIYVPC; -.
DR PhylomeDB; P0A7A7; -.
DR BioCyc; EcoCyc:GLYCEROL-3-P-ACYLTRANSFER-MON; -.
DR BioCyc; MetaCyc:GLYCEROL-3-P-ACYLTRANSFER-MON; -.
DR SABIO-RK; P0A7A7; -.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:P0A7A7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IMP:EcoliWiki.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:EcoliWiki.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR03703; plsB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..807
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195218"
FT MOTIF 306..311
FT /note="HXXXXD motif"
FT MUTAGEN 306
FT /note="H->A: Abolishes acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527,
FT ECO:0000269|PubMed:9515909"
FT MUTAGEN 306
FT /note="H->G: Reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527,
FT ECO:0000269|PubMed:9515909"
FT MUTAGEN 308
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 311
FT /note="D->A: Prevents assembly into the membrane,
FT suggesting that it participates in folding."
FT /evidence="ECO:0000269|PubMed:10231527,
FT ECO:0000269|PubMed:9515909"
FT MUTAGEN 311
FT /note="D->G: Strongly reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527,
FT ECO:0000269|PubMed:9515909"
FT MUTAGEN 349
FT /note="A->T: In plsB26; results in high KM for glycerol-3-
FT phosphate and reduced specific activity."
FT /evidence="ECO:0000269|PubMed:10074094"
FT MUTAGEN 351
FT /note="F->A: Strongly reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 352
FT /note="I->A: Reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 354
FT /note="R->C: Reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 354
FT /note="R->K: No effect."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 385
FT /note="E->R: Strongly reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 386
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 386
FT /note="G->L: Reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 389
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:10231527"
FT MUTAGEN 421
FT /note="P->S: Reduced acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10231527"
SQ SEQUENCE 807 AA; 91381 MW; D6FC6892981D7EFE CRC64;
MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP IMYVLPYNSK ADLLTLRAQC
LAHDLPDPLE PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE SIKLFHDYLD LHRSNPNLDV
QMVPVSVMFG RAPGREKGEV NPPLRMLNGV QKFFAVLWLG RDSFVRFSPS VSLRRMADEH
GTDKTIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASRAIAKAV EDEARSKKIS
HEKAQQNAIA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEL
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLI
PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR NLGQGYVNFG EPMPLMTYLN
QHVPDWRESI DPIEAVRPAW LTPTVNNIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL
TREQLTEQLN CYLDLMRNVP YSTDSTVPSA SASELIDHAL QMNKFEVEKD TIGDIIILPR
EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISRDVLME HVNVLYPMLK AELFLRWDRD
ELPDVIDALA NEMQRQGLIT LQDDELHINP AHSRTLQLLA AGARETLQRY AITFWLLSAN
PSINRGTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DSGDAEPAET
MKVYQLLAEL ITSDVRLTIE SATQGEG
