Q8X6J8 (AAS_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein aas

Including the following 2 domains:

1. 2-acylglycerophosphoethanolamine acyltransferase
   EC=2.3.1.40
   Alternative name(s):
   2-acyl-GPE acyltransferase
   Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
2. Acyl-[acyl-carrier-protein] synthetase
   EC=6.2.1.20
   Alternative name(s):
   Acyl-ACP synthetase
   Long-chain-fatty-acid--[acyl-carrier-protein] ligase

Gene names

Name:	aas
Ordered Locus Names:	Z4154, ECs3693

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
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. HAMAP MF_01162
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 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 Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Acyltransferase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: InterPro phospholipid biosynthetic 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: EC long-chain fatty acid [acyl-carrier-protein] ligase 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 – 719	719	Bifunctional protein aas HAMAP MF_01162		PRO_0000193047
Regions
	Transmembrane	258 – 277	20	Helical; Potential
	Transmembrane	409 – 433	25	Helical; 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)
	Q8X6J8 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 786640F7D3330B7C	FASTA	719	80,764
	10 20 30 40 50 60 MLFSFFRNLC RVLYRVRVTG DPQALKGERV 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 EMPDAPRARD 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 VDEVEQHDE

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG57948.1. BA000007 Genomic DNA. Translation: BAB37116.1.
PIR	E91090. H85935.
RefSeq	NP_289389.1. NC_002655.2. NP_311720.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X6J8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000024437; EBESCP00000023330; EBESCG00000023491. EBESCT00000057987; EBESCP00000055815; EBESCG00000057035.
GeneID	916493. 958304.
GenomeReviews	Gene locus Z4154 in contig AE005174_GR. Gene locus ECs3693 in contig BA000007_GR.
KEGG	ece:Z4154. ecs:ECs3693.
PATRIC	18356877. VBIEscCol44059_3618.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008805.
HOGENOM	HBG361068.
OMA	ANWVYLE.
ProtClustDB	PRK08043.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3693-MONOMER.
Family and domain databases
HAMAP	MF_01162. Aas. [Tree]
InterPro	IPR002123. Acyltransferase. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR023775. Bifunctional_Aas. [Graphical view]
KO	K05939.
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_ECO57

Accession

Primary (citable) accession number: Q8X6J8
Secondary accession number(s): Q7AB50

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program