Reviewed, UniProtKB/Swiss-Prot P26647 (PLSC_ECOLI)

Names and origin

Protein names

Recommended name:
    1-acyl-sn-glycerol-3-phosphate acyltransferase
      Short name=1-AGP acyltransferase
      Short name=1-AGPAT
    EC=2.3.1.51
Alternative name(s):
    Lysophosphatidic acid acyltransferase
      Short name=LPAAT

Gene names

Name:	plsC
Synonyms:	parF
Ordered Locus Names:	b3018, JW2986

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	245 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-acyl-carrier-protein as the fatty acyl donor.
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular location	Cell inner membrane; Peripheral membrane protein.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Molecular function	Acyltransferase Transferase
PTM	Formylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 245	245	1-acyl-sn-glycerol-3-phosphate acyltransferase		PRO_0000208168
Regions
	Motif	73 – 78	6	HXXXXD motif
Amino acid modifications
	Modified residue	1	1	N-formylmethionine Probable Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P26647-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: E9A1E697E7149838	FASTA	245	27,453
	10 20 30 40 50 60 MLYIFRLIIT VIYSILVCVF GSIYCLFSPR NPKHVATFGH MFGRLAPLFG LKVECRKPTD 70 80 90 100 110 120 AESYGNAIYI ANHQNNYDMV TASNIVQPPT VTVGKKSLLW IPFFGQLYWL TGNLLIDRNN 130 140 150 160 170 180 RTKAHGTIAE VVNHFKKRRI SIWMFPEGTR SRGRGLLPFK TGAFHAAIAA GVPIIPVCVS 190 200 210 220 230 240 TTSNKINLNR LHNGLVIVEM LPPIDVSQYG KDQVRELAAH CRSIMEQKIA ELDKEVAERE AAGKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC)." Coleman J. Mol. Gen. Genet. 232:295-303(1992) [PubMed: 1557036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7.
[2]	"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.
[3]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M63491 Genomic DNA. Translation: AAA24397.1. U28377 Genomic DNA. Translation: AAA69186.1. U00096 Genomic DNA. Translation: AAC76054.1. AP009048 Genomic DNA. Translation: BAE77074.1.
PIR	S20460.
RefSeq	AP_003568.1. NP_417490.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	947496.
GenomeReviews	Gene locus JW2986 in contig AP009048_GR. Gene locus b3018 in contig U00096_GR.
KEGG	ecj:JW2986. eco:b3018.
Organism-specific databases
EchoBASE	EB1351.
EcoGene	EG11377. plsC.
CMR	Search...
Phylogenomic databases
HOGENOM	P26647.
OMA	P26647. KSLVWIP.
Enzyme and pathway databases
BioCyc	EcoCyc:1-ACYLGLYCEROL-3-P-ACYLTRANSFER-MON. MetaCyc:1-ACYLGLYCEROL-3-P-ACYLTRANSFER-MON.
Family and domain databases
InterPro	IPR002123. Acyltransferase. IPR004552. AGP_acyltrans. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
TIGRFAMs	TIGR00530. AGP_acyltrn. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PLSC_ECOLI

Accession

Primary (citable) accession number: P26647
Secondary accession number(s): Q2M9I2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)