Bifunctional protein aas - Escherichia coli (strain K12)

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P31119 (AAS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional protein aas

Including the following 2 domains:

2-acylglycerophosphoethanolamine acyltransferase
EC=2.3.1.40
Alternative name(s):
2-acyl-GPE acyltransferase
Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
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:	b2836, JW2804

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
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 Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Acyltransferase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from genetic interaction Ref.5. Source: EcoliWiki phospholipid biosynthetic process Inferred from genetic interaction Ref.5. Source: EcoliWiki
Cellular component	integral to membrane Inferred from direct assay. Source: EcoliWiki 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 direct assay. Source: EcoliWiki long-chain fatty acid [acyl-carrier-protein] ligase activity Inferred from direct assay. Source: EcoliWiki
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

Helical; Potential

Transmembrane

409 – 433

Helical; Potential

Region

15 – 138

124

Acyltransferase HAMAP MF_01162

Region

233 – 646

414

AMP-binding HAMAP MF_01162

Sites

Active site

Experimental info

Mutagenesis

H → A: Loss of 2-acyl-GPE acyltransferase activity; retains acyl-ACP synthetase activity. Ref.6

Sequence conflict

15 – 16

RV → AL in AAA17550. Ref.1

Sequence conflict

202

P → S in AAA17550. Ref.1

Sequence conflict

281

M → I in AAT42454. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P31119 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: F4F1021E57835EB2
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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

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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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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	NP_417313.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P31119.
SMR	P31119. Positions 206-696.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9025N.
IntAct	P31119. 9 interactions.
MINT	MINT-1308806.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001503; EBESCP00000001503; EBESCG00000001249. EBESCT00000016594; EBESCP00000015885; EBESCG00000015653.
GeneID	947315.
GenomeReviews	Gene locus JW2804 in contig AP009048_GR. Gene locus b2836 in contig U00096_GR.
KEGG	ecj:JW2804. eco:b2836.
PATRIC	32121090. VBIEscCol129921_2934.
Organism-specific databases
EchoBASE	EB1630.
EcoGene	EG11679. aas.
Phylogenomic databases
eggNOG	COG0318.
GeneTree	EBGT00050000008805.
HOGENOM	HBG361068.
OMA	ANWVYLE.
PhylomeDB	P31119.
ProtClustDB	PRK08043.
Enzyme and pathway databases
BioCyc	EcoCyc:AAS-MONOMER. MetaCyc:AAS-MONOMER.
BRENDA	2.3.1.40. 2026.
Gene expression databases
Genevestigator	P31119.
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_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:	January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents