[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7. PubMed=1557036 [NCBI, ExPASy, EBI, Israel, Japan] Coleman J.; "Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC)."; Mol. Gen. Genet. 232:295-303(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

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).
SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M63491; AAA24397.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U28377; AAA69186.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76054.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77074.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S20460; S20460.

RefSeq

AP_003568.1; -.
NP_417490.1; -.

3D structure databases

ModBase

P26647.

Enzyme and pathway databases

BioCyc

EcoCyc:1-ACYLGLYCEROL-3-P-ACYLTRANSFER-MON; -.
MetaCyc:1-ACYLGLYCEROL-3-P-ACYLTRANSFER-MON; -.

Organism-specific databases

EchoBASE

EB1351; -.

EcoGene

EG11377; plsC.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0003841;	Molecular function: 1-acylglycerol-3-phosphate O-acyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008654;	Biological process: phospholipid biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002123; Acyltransferase.
IPR004552; AGP_acyltrans.
Graphical view of domain structure.

Pfam

PF01553; Acyltransferase; 1.
Pfam graphical view of domain structure.

SMART

SM00563; PlsC; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00530; AGP_acyltrn; 1.

Genome annotation databases

GeneID

947496; -.

GenomeReviews

U00096_GR; b3018.
AP009048_GR; JW2986.

KEGG

ecj:JW2986; -.
eco:b3018; -.

Phylogenomic databases

HOGENOM

P26647; -.

Genome annotation databases

CMR

P26647; b3018.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Formylation; Membrane; Phospholipid biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 245`	`245`	`1-acyl-sn-glycerol-3-phosphate acyltransferase.`	`PRO_0000208168`
`MOTIF`	`73 78`	`6`	`HXXXXD motif.`
`MOD_RES`	`1 1`		`N-formylmethionine (Probable).`

Sequence information

Length: 245 AA [This is the length of the unprocessed precursor]

Molecular weight: 27453 Da [This is the MW of the unprocessed precursor]

CRC64: E9A1E697E7149838 [This is a checksum on the sequence]

        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

P26647 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools