Glycerol-3-phosphate acyltransferase - Escherichia coli (strain K12)

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P0A7A7 (PLSB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate acyltransferase
Short name=GPAT
EC=2.3.1.15

Gene names

Name:	plsB
Ordered Locus Names:	b4041, JW4001

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 Ref.15
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393
Subunit structure	Interacts with ACP, YbgC and PssA, forming altogether a complex at the inner membrane. Ref.14
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Ref.8 Ref.14.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. HAMAP MF_00393
Sequence similarities	Belongs to the GPAT/DAPAT family.
Biophysicochemical properties	Kinetic parameters: K_M=49 µM for glycerol-3-phosphate Ref.11 Ref.13 V_max=13.1 nmol/min/mg enzyme with glycerol-3-phosphate as substrate pH dependence: Optimum pH is 8.5.
Sequence caution	The sequence AAC43135.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from mutant phenotype. Source: EcoliWiki phospholipid biosynthetic process Inferred from mutant phenotype. Source: EcoliWiki
Cellular component	integral to plasma membrane Inferred from direct assay Ref.2 Ref.10. Source: EcoliWiki
Molecular function	glycerol-3-phosphate O-acyltransferase activity Inferred from mutant phenotype Ref.9. Source: EcoliWiki protein binding Inferred from physical interaction Ref.14. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
acpP	P0A6A8	3	EBI-542961,EBI-542566

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed HAMAP MF_00393

Chain

2 – 807

806

Glycerol-3-phosphate acyltransferase HAMAP MF_00393

PRO_0000195218

Regions

Motif

306 – 311

HXXXXD motif HAMAP MF_00393

Experimental info

Mutagenesis

306

H → A: Abolishes acyltransferase activity. Ref.12 Ref.13

Mutagenesis

306

H → G: Reduced acyltransferase activity. Ref.12 Ref.13

Mutagenesis

308

S → A: No effect. Ref.13

Mutagenesis

311

D → A: Prevents assembly into the membrane, suggesting that it paticipates to folding. Ref.12 Ref.13

Mutagenesis

311

D → G: Strongly reduced acyltransferase activity. Ref.12 Ref.13

Mutagenesis

349

A → T in plsB26; results in high KM for glycerol-3-phosphate and reduced specific activity. Ref.2

Mutagenesis

351

F → A: Strongly reduced acyltransferase activity. Ref.13

Mutagenesis

352

I → A: Reduced acyltransferase activity. Ref.13

Mutagenesis

354

R → C: Reduced acyltransferase activity. Ref.13

Mutagenesis

354

R → K: No effect. Ref.13

Mutagenesis

385

E → R: Strongly reduced acyltransferase activity. Ref.13

Mutagenesis

386

G → A: No effect. Ref.13

Mutagenesis

386

G → L: Reduced acyltransferase activity. Ref.13

Mutagenesis

389

S → A: No effect. Ref.13

Mutagenesis

421

P → S: Reduced acyltransferase activity. Ref.13

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7A7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D6FC6892981D7EFE
Show »

FASTA

807

91,381

        10         20         30         40         50         60 
MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP IMYVLPYNSK ADLLTLRAQC 

        70         80         90        100        110        120 
LAHDLPDPLE PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE SIKLFHDYLD LHRSNPNLDV 

       130        140        150        160        170        180 
QMVPVSVMFG RAPGREKGEV NPPLRMLNGV QKFFAVLWLG RDSFVRFSPS VSLRRMADEH 

       190        200        210        220        230        240 
GTDKTIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASRAIAKAV EDEARSKKIS 

       250        260        270        280        290        300 
HEKAQQNAIA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEL 

       310        320        330        340        350        360 
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK 

       370        380        390        400        410        420 
LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLI 

       430        440        450        460        470        480 
PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR NLGQGYVNFG EPMPLMTYLN 

       490        500        510        520        530        540 
QHVPDWRESI DPIEAVRPAW LTPTVNNIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL 

       550        560        570        580        590        600 
TREQLTEQLN CYLDLMRNVP YSTDSTVPSA SASELIDHAL QMNKFEVEKD TIGDIIILPR 

       610        620        630        640        650        660 
EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISRDVLME HVNVLYPMLK AELFLRWDRD 

       670        680        690        700        710        720 
ELPDVIDALA NEMQRQGLIT LQDDELHINP AHSRTLQLLA AGARETLQRY AITFWLLSAN 

       730        740        750        760        770        780 
PSINRGTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DSGDAEPAET 

       790        800 
MKVYQLLAEL ITSDVRLTIE SATQGEG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 6309817] [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: 10074094] [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: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 1644758] [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: 6350296] [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: 4943977] [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: 6251087] [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: 6997313] [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: 7026564] [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: 9515909] [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: 10231527] [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: 16294310] [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: 17645809] [Abstract] Cited for: FUNCTION IN PHOSPHOLIPID BIOSYNTHESIS. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	XUECAG. A00565.
RefSeq	NP_418465.4. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A7A7.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29380N.
IntAct	P0A7A7. 36 interactions.
MINT	MINT-1221841.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000002684; EBESCP00000002684; EBESCG00000002190. EBESCT00000017037; EBESCP00000016328; EBESCG00000016096.
GeneID	948541.
GenomeReviews	Gene locus JW4001 in contig AP009048_GR. Gene locus b4041 in contig U00096_GR.
KEGG	ecj:JW4001. eco:b4041.
PATRIC	32123619. VBIEscCol129921_4158.
Organism-specific databases
EchoBASE	EB0733.
EcoGene	EG10740. plsB.
Phylogenomic databases
eggNOG	COG2937.
GeneTree	EBGT00050000010697.
HOGENOM	HBG296590.
OMA	WNKLYQG.
ProtClustDB	PRK04974.
Enzyme and pathway databases
BioCyc	EcoCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER. MetaCyc:GLYCEROL-3-P-ACYLTRANSFER-MONOMER.
Gene expression databases
Genevestigator	P0A7A7.
Family and domain databases
HAMAP	MF_00393. Glyc3P_acyltrans. [Tree]
InterPro	IPR002123. Acyltransferase. IPR022284. G3P_O-AcylTrfase. [Graphical view]
KO	K00631.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
PIRSF	PIRSF000437. GPAT_DHAPAT. 1 hit.
SMART	SM00563. PlsC. 1 hit. [Graphical view]
TIGRFAMs	TIGR03703. PlsB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PLSB_ECOLI

Accession

Primary (citable) accession number: P0A7A7
Secondary accession number(s): P00482, Q2M6R3, Q9S683

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents