Reviewed, UniProtKB/Swiss-Prot P31119 (AAS_ECOLI)

Names and origin

Protein names

Recommended name:
    Bifunctional protein aas
Including the following 2 domains:
    1- Recommended name:
            2-acylglycerophosphoethanolamine acyltransferase
              EC=2.3.1.40
        Alternative name(s):
            Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
            2-acyl-GPE acyltransferase
    2- Recommended name:
            Acyl-[acyl-carrier-protein] synthetase
              EC=6.2.1.20
        Alternative name(s):
            Long-chain-fatty-acid--[acyl-carrier-protein] ligase
            Acyl-ACP synthetase

Gene names

Name:	aas
Ordered Locus Names:	b2836, JW2804

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.5
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. HAMAP MF_01162 ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein]. HAMAP MF_01162
Subcellular location	Cell inner membrane; Multi-pass membrane protein. HAMAP MF_01162
Sequence similarities	In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Acyltransferase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity Inferred from electronic annotation. Source: HAMAP long-chain-fatty-acid-[acyl-carrier-protein] ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 719	719	Bifunctional protein aas HAMAP MF_01162		PRO_0000193046
Regions
	Transmembrane	258 – 277	20	Potential
	Transmembrane	409 – 433	25	Potential
	Region	15 – 138	124	Acyltransferase HAMAP MF_01162
	Region	233 – 646	414	AMP-binding HAMAP MF_01162
Sites
	Active site	36	1	HAMAP MF_01162
Experimental info
	Mutagenesis	36	1	H → A: Loss of 2-acyl-GPE acyltransferase activity; retains acyl-ACP synthetase activity. Ref.6
	Sequence conflict	15 – 16	2	RV → AL in AAA17550. Ref.1
	Sequence conflict	202	1	P → S in AAA17550. Ref.1
	Sequence conflict	281	1	M → I in AAT42454. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P31119-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: F4F1021E57835EB2	FASTA	719	80,700
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and function of the aas gene in Escherichia coli." Jackowski S., Jackson P.D., Rock C.O. J. Biol. Chem. 269:2921-2928(1994) [PubMed: 8300626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[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.
[4]	"Rates of DNA sequence evolution in experimental populations of Escherichia coli during 20,000 generations." Lenski R.E., Winkworth C.L., Riley M.A. J. Mol. Evol. 56:498-508(2003) [PubMed: 12664169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-311. Strain: B / Bc251.
[5]	"Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity." Hsu L., Jackowski S., Rock C.O. J. Biol. Chem. 266:13783-13788(1991) [PubMed: 1649829] [Abstract] Cited for: FUNCTION. Strain: K12.
[6]	"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-36. Strain: K12.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L14681 Unassigned DNA. Translation: AAA17550.1. U29581 Genomic DNA. Translation: AAB40483.1. U00096 Genomic DNA. Translation: AAC75875.1. AP009048 Genomic DNA. Translation: BAE76905.1. AY625100 Genomic DNA. Translation: AAT42454.1.
PIR	E65066.
RefSeq	AP_003399.1. NP_417313.1.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9025N.
Genome annotation databases
GeneID	947315.
GenomeReviews	Gene locus JW2804 in contig AP009048_GR. Gene locus b2836 in contig U00096_GR.
KEGG	ecj:JW2804. eco:b2836.
Organism-specific databases
EchoBASE	EB1630.
EcoGene	EG11679. aas.
CMR	Search...
Phylogenomic databases
HOGENOM	P31119.
OMA	P31119. KGYLRVE.
Enzyme and pathway databases
BioCyc	EcoCyc:AAS-MON. MetaCyc:AAS-MON.
BRENDA	2.3.1.40. 246.
Family and domain databases
HAMAP	MF_01162. [Tree]
InterPro	IPR002123. Acyltransferase. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. PF00501. AMP-binding. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAS_ECOLI

Accession

Primary (citable) accession number: P31119
Secondary accession number(s): Q2MA01, Q46935, Q6IU49

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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