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Protein

Glycerol-3-phosphate acyltransferase

Gene

plsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor.2 Publications

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.

Kineticsi

  1. KM=49 µM for glycerol-3-phosphate2 Publications
  1. Vmax=13.1 nmol/min/mg enzyme with glycerol-3-phosphate as substrate2 Publications

pH dependencei

Optimum pH is 8.5.2 Publications

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase (plsB)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC)
  3. Phosphatidate cytidylyltransferase (cdsA)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • glycerol-3-phosphate O-acyltransferase activity Source: EcoliWiki

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • fatty acid metabolic process Source: EcoliWiki
  • phospholipid biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER.
ECOL316407:JW4001-MONOMER.
MetaCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER.
SABIO-RKP0A7A7.
UniPathwayiUPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase (EC:2.3.1.15)
Short name:
GPAT
Gene namesi
Name:plsB
Ordered Locus Names:b4041, JW4001
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10740. plsB.

Subcellular locationi

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi306 – 3061H → A: Abolishes acyltransferase activity. 2 Publications
Mutagenesisi306 – 3061H → G: Reduced acyltransferase activity. 2 Publications
Mutagenesisi308 – 3081S → A: No effect. 1 Publication
Mutagenesisi311 – 3111D → A: Prevents assembly into the membrane, suggesting that it paticipates to folding. 2 Publications
Mutagenesisi311 – 3111D → G: Strongly reduced acyltransferase activity. 2 Publications
Mutagenesisi349 – 3491A → T in plsB26; results in high KM for glycerol-3-phosphate and reduced specific activity. 1 Publication
Mutagenesisi351 – 3511F → A: Strongly reduced acyltransferase activity. 1 Publication
Mutagenesisi352 – 3521I → A: Reduced acyltransferase activity. 1 Publication
Mutagenesisi354 – 3541R → C: Reduced acyltransferase activity. 1 Publication
Mutagenesisi354 – 3541R → K: No effect. 1 Publication
Mutagenesisi385 – 3851E → R: Strongly reduced acyltransferase activity. 1 Publication
Mutagenesisi386 – 3861G → A: No effect. 1 Publication
Mutagenesisi386 – 3861G → L: Reduced acyltransferase activity. 1 Publication
Mutagenesisi389 – 3891S → A: No effect. 1 Publication
Mutagenesisi421 – 4211P → S: Reduced acyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 807806Glycerol-3-phosphate acyltransferasePRO_0000195218Add
BLAST

Proteomic databases

EPDiP0A7A7.
PaxDbiP0A7A7.
PRIDEiP0A7A7.

Interactioni

Subunit structurei

Interacts with ACP, YbgC and PssA, forming altogether a complex at the inner membrane.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
acpPP0A6A83EBI-542961,EBI-542566

Protein-protein interaction databases

BioGridi4261720. 245 interactions.
DIPiDIP-29380N.
IntActiP0A7A7. 36 interactions.
MINTiMINT-1221841.
STRINGi511145.b4041.

Structurei

3D structure databases

ProteinModelPortaliP0A7A7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi306 – 3116HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.

Sequence similaritiesi

Belongs to the GPAT/DAPAT family.Curated

Phylogenomic databases

eggNOGiENOG4105E55. Bacteria.
COG2937. LUCA.
HOGENOMiHOG000218231.
InParanoidiP0A7A7.
KOiK00631.
OMAiEVIYVPC.
OrthoDBiEOG6B625B.
PhylomeDBiP0A7A7.

Family and domain databases

HAMAPiMF_00393. Glyc3P_acyltrans.
InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 2 hits.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03703. plsB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP IMYVLPYNSK
60 70 80 90 100
ADLLTLRAQC LAHDLPDPLE PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE
110 120 130 140 150
SIKLFHDYLD LHRSNPNLDV QMVPVSVMFG RAPGREKGEV NPPLRMLNGV
160 170 180 190 200
QKFFAVLWLG RDSFVRFSPS VSLRRMADEH GTDKTIAQKL ARVARMHFAR
210 220 230 240 250
QRLAAVGPRL PARQDLFNKL LASRAIAKAV EDEARSKKIS HEKAQQNAIA
260 270 280 290 300
LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEL
310 320 330 340 350
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF
360 370 380 390 400
FIRRTFKGNK LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG
410 420 430 440 450
TLSMTIQAML RGGTRPITLI PIYIGYEHVM EVGTYAKELR GATKEKESLP
460 470 480 490 500
QMLRGLSKLR NLGQGYVNFG EPMPLMTYLN QHVPDWRESI DPIEAVRPAW
510 520 530 540 550
LTPTVNNIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL TREQLTEQLN
560 570 580 590 600
CYLDLMRNVP YSTDSTVPSA SASELIDHAL QMNKFEVEKD TIGDIIILPR
610 620 630 640 650
EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISRDVLME HVNVLYPMLK
660 670 680 690 700
AELFLRWDRD ELPDVIDALA NEMQRQGLIT LQDDELHINP AHSRTLQLLA
710 720 730 740 750
AGARETLQRY AITFWLLSAN PSINRGTLEK ESRTVAQRLS VLHGINAPEF
760 770 780 790 800
FDKAVFSSLV LTLRDEGYIS DSGDAEPAET MKVYQLLAEL ITSDVRLTIE

SATQGEG
Length:807
Mass (Da):91,381
Last modified:January 23, 2007 - v2
Checksum:iD6FC6892981D7EFE
GO

Sequence cautioni

The sequence AAC43135.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00127 Genomic DNA. Translation: AAA24395.1.
AF106625 Genomic DNA. Translation: AAD20588.1.
U00006 Genomic DNA. Translation: AAC43135.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77011.2.
AP009048 Genomic DNA. Translation: BAE78043.1.
M93413 Genomic DNA. Translation: AAA24718.1.
M93136 Genomic DNA. Translation: AAA24713.1.
PIRiA00565. XUECAG.
RefSeqiNP_418465.4. NC_000913.3.
WP_000017354.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77011; AAC77011; b4041.
BAE78043; BAE78043; BAE78043.
GeneIDi948541.
KEGGiecj:JW4001.
eco:b4041.
PATRICi32123619. VBIEscCol129921_4158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00127 Genomic DNA. Translation: AAA24395.1.
AF106625 Genomic DNA. Translation: AAD20588.1.
U00006 Genomic DNA. Translation: AAC43135.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77011.2.
AP009048 Genomic DNA. Translation: BAE78043.1.
M93413 Genomic DNA. Translation: AAA24718.1.
M93136 Genomic DNA. Translation: AAA24713.1.
PIRiA00565. XUECAG.
RefSeqiNP_418465.4. NC_000913.3.
WP_000017354.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A7A7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261720. 245 interactions.
DIPiDIP-29380N.
IntActiP0A7A7. 36 interactions.
MINTiMINT-1221841.
STRINGi511145.b4041.

Proteomic databases

EPDiP0A7A7.
PaxDbiP0A7A7.
PRIDEiP0A7A7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77011; AAC77011; b4041.
BAE78043; BAE78043; BAE78043.
GeneIDi948541.
KEGGiecj:JW4001.
eco:b4041.
PATRICi32123619. VBIEscCol129921_4158.

Organism-specific databases

EchoBASEiEB0733.
EcoGeneiEG10740. plsB.

Phylogenomic databases

eggNOGiENOG4105E55. Bacteria.
COG2937. LUCA.
HOGENOMiHOG000218231.
InParanoidiP0A7A7.
KOiK00631.
OMAiEVIYVPC.
OrthoDBiEOG6B625B.
PhylomeDBiP0A7A7.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BioCyciEcoCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER.
ECOL316407:JW4001-MONOMER.
MetaCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER.
SABIO-RKP0A7A7.

Miscellaneous databases

PROiP0A7A7.

Family and domain databases

HAMAPiMF_00393. Glyc3P_acyltrans.
InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 2 hits.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03703. plsB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequences encoding plsB and dgk loci of Escherichia coli."
    Lightner V.A., Bell R.M., Modrich P.
    J. Biol. Chem. 258:10856-10861(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A missense mutation accounts for the defect in the glycerol-3-phosphate acyltransferase expressed in the plsB26 mutant."
    Heath R.J., Rock C.O.
    J. Bacteriol. 181:1944-1946(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ALA-349.
    Strain: K12.
  3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase."
    Nichols B.P., Green J.M.
    J. Bacteriol. 174:5309-5316(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 781-807.
    Strain: K12.
  7. "Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase."
    Green P.R., Vanaman T.C., Modrich P., Bell R.M.
    J. Biol. Chem. 258:10862-10866(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  8. "Distribution of phospholipid-synthesizing enzymes in the wall and membrane subfractions of the envelope of Escherichia coli."
    White D.A., Albright F.R., Lennarz W.J., Schnaitman C.A.
    Biochim. Biophys. Acta 249:636-642(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Membrane phospholipid synthesis in Escherichia coli. Cloning of a structural gene (plsB) of the sn-glycerol-3-phosphate acyl/transferase."
    Lightner V.A., Larson T.J., Tailleur P., Kantor G.D., Raetz C.R., Bell R.M., Modrich P.
    J. Biol. Chem. 255:9413-9420(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
    Strain: K12.
  10. "Membrane phospholipid synthesis in Escherichia coli. Identification of the sn-glycerol-3-phosphate acyltransferase polypeptide as the plsB gene product."
    Larson T.J., Lightner V.A., Green P.R., Modrich P., Bell R.M.
    J. Biol. Chem. 255:9421-9426(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12.
  11. "Membrane phospholipid synthesis in Escherichia coli. Purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase."
    Green P.R., Merrill A.H. Jr., Bell R.M.
    J. Biol. Chem. 256:11151-11159(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FATTY ACYL DONOR SPECIFICITY.
  12. "A conserved histidine is essential for glycerolipid acyltransferase catalysis."
    Heath R.J., Rock C.O.
    J. Bacteriol. 180:1425-1430(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-306 AND ASP-311.
    Strain: K12.
  13. "Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction."
    Lewin T.M., Wang P., Coleman R.A.
    Biochemistry 38:5764-5771(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-306; SER-308; ASP-311; PHE-351; ILE-352; ARG-354; GLU-385; GLY-386; SER-389 AND PRO-421.
    Strain: K12.
  14. "A protein network for phospholipid synthesis uncovered by a variant of the tandem affinity purification method in Escherichia coli."
    Gully D., Bouveret E.
    Proteomics 6:282-293(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ACP; YBGC AND PSSA.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  15. "Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli."
    Yoshimura M., Oshima T., Ogasawara N.
    BMC Microbiol. 7:69-69(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHOLIPID BIOSYNTHESIS.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiPLSB_ECOLI
AccessioniPrimary (citable) accession number: P0A7A7
Secondary accession number(s): P00482, Q2M6R3, Q9S683
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.