Reviewed, UniProtKB/Swiss-Prot A8A3X0 (AAS_ECOHS)

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:	EcHS_A2983

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [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	Inferred from homology.

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 By similarity.
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 By similarity.
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_1000065635
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	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8A3X0-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: A44ABA7042959F6D	FASTA	719	80,682
	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 IPAMMNYTAG 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

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000802 Genomic DNA. Translation: ABV07224.1.
RefSeq	YP_001459607.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5595493.
GenomeReviews	Gene locus EcHS_A2983 in contig CP000802_GR.
KEGG	ecx:EcHS_A2983.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A8A3X0. KGYLRVE.
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_ECOHS

Accession

Primary (citable) accession number: A8A3X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	June 16, 2009
This is version 13 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)