2-acylglycerophosphoethanolamine acyltransferase
     (EC 2.3.1.40)
     (Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase)
     (2-acyl-GPE acyltransferase)
Acyl-[acyl-carrier-protein] synthetase
     (EC 6.2.1.20)
     (Long-chain-fatty-acid--[acyl-carrier-protein] ligase)
     (Acyl-ACP synthetase)

Gene name

	Name:	aas
	OrderedLocusNames:	b2836, JW2804

From

Escherichia coli (strain K12)

[TaxID: 83333]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=8300626 [NCBI, ExPASy, EBI, Israel, Japan] Jackowski S., Jackson P.D., Rock C.O.; "Sequence and function of the aas gene in Escherichia coli."; J. Biol. Chem. 269:2921-2928(1994).
[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).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-311. STRAIN=B / Bc251; DOI=10.1007/s00239-002-2423-0; PubMed=12664169 [NCBI, ExPASy, EBI, Israel, Japan] Lenski R.E., Winkworth C.L., Riley M.A.; "Rates of DNA sequence evolution in experimental populations of Escherichia coli during 20,000 generations."; J. Mol. Evol. 56:498-508(2003).
[5]	FUNCTION. STRAIN=K12; PubMed=1649829 [NCBI, ExPASy, EBI, Israel, Japan] Hsu L., Jackowski S., Rock C.O.; "Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity."; J. Biol. Chem. 266:13783-13788(1991).
[6]	MUTAGENESIS OF HIS-36. STRAIN=K12; PubMed=9515909 [NCBI, ExPASy, EBI, Israel, Japan] Heath R.J., Rock C.O.; "A conserved histidine is essential for glycerolipid acyltransferase catalysis."; J. Bacteriol. 180:1425-1430(1998).

Comments

FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine.
CATALYTIC ACTIVITY: ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein].
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family.
SIMILARITY: In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme 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

L14681; AAA17550.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U29581; AAB40483.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75875.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76905.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY625100; AAT42454.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E65066; E65066.

RefSeq

AP_003399.1; -.
NP_417313.1; -.

3D structure databases

HSSP

P08659; 1LCI. [HSSP ENTRY / PDB]

ModBase

P31119.

Protein-protein interaction databases

DIP

DIP:9025N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:AAS-MON; -.
MetaCyc:AAS-MON; -.

Organism-specific databases

EchoBASE

EB1630; -.

EcoGene

EG11679; aas.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0008779;	Molecular function: acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008922;	Molecular function: long-chain-fatty-acid-[acyl-carrier-protein] ligase activity (inferred from electronic annotation from HAMAP).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_01162; -; 1.
PBIL [Tree]

InterPro

IPR002123; Acyltransferase.
IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.

Pfam

PF01553; Acyltransferase; 1.
PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.

PRINTS

PR00154; AMPBINDING.

SMART

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

PROSITE

PS00455; AMP_BINDING; 1.

Genome annotation databases

GeneID

947315; -.

GenomeReviews

AP009048_GR; JW2804.
U00096_GR; b2836.

KEGG

ecj:JW2804; -.
eco:b2836; -.

Phylogenomic databases

HOGENOM

P31119; -.

Genome annotation databases

CMR

P31119; b2836.

Other

ProtoNet

P31119.

UniRef

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

Keywords

Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; Ligase; Membrane; Multifunctional enzyme; Nucleotide-binding; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 719`	`719`	`Bifunctional protein aas.`	`PRO_0000193046`
`TRANSMEM`	`258 277`	`20`	`Potential.`
`TRANSMEM`	`409 433`	`25`	`Potential.`
`REGION`	`15 138`	`124`	`Acyltransferase.`
`REGION`	`233 646`	`414`	`AMP-binding.`
`ACT_SITE`	`36 36`
`MUTAGEN`	`36 36`		`H->A: Loss of 2-acyl-GPE acyltransferase activity; retains acyl-ACP synthetase activity.`
`CONFLICT`	`15 16`		`RV -> AL (in Ref. 1; AAA17550).`
`CONFLICT`	`202 202`		`P -> S (in Ref. 1; AAA17550).`
`CONFLICT`	`281 281`		`M -> I (in Ref. 4; AAT42454).`

Sequence information

Length: 719 AA [This is the length of the unprocessed precursor]

Molecular weight: 80700 Da [This is the MW of the unprocessed precursor]

CRC64: F4F1021E57835EB2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLFSFFRNLC RVLYRVRVTG DTQALKGERV LITPNHVSFI DGILLGLFLP VRPVFAVYTS 

        70         80         90        100        110        120 
ISQQWYMRWL KSFIDFVPLD PTQPMAIKHL VRLVEQGRPV VIFPEGRITT TGSLMKIYDG 

       130        140        150        160        170        180 
AGFVAAKSGA TVIPVRIEGA ELTHFSRLKG LVKRRLFPQI TLHILPPTQV AMPDAPRARD 

       190        200        210        220        230        240 
RRKIAGEMLH QIMMEARMAV RPRETLYESL LSAMYRFGAG KKCVEDVNFT PDSYRKLLTK 

       250        260        270        280        290        300 
TLFVGRILEK YSVEGERIGL MLPNAGISAA VIFGAIARRR MPAMMNYTAG VKGLTSAITA 

       310        320        330        340        350        360 
AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFA HLLMPRLAQV 

       370        380        390        400        410        420 
KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTTNDRFM SALPLFHSFG 

       430        440        450        460        470        480 
LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRSCTVLF GTSTFLGHYA RFANPYDFYR 

       490        500        510        520        530        540 
LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM 

       550        560        570        580        590        600 
DARLLSVPGI EEGGRLQLKG PNIMNGYLRV EKPGVLEVPT AENVRGEMER GWYDTGDIVR 

       610        620        630        640        650        660 
FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA SKGEALVLFT 

       670        680        690        700        710 
TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG KPDFVTLKSW VDEAEQHDE

P31119 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