Bifunctional protein aas - Escherichia coli O45:K1 (strain S88 / ExPEC)

Preferred order of sections

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:	ECS88_3131

Organism

Escherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585035 [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-Rule 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-Rule MF_01162 ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein]. HAMAP-Rule MF_01162
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule 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: 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-Rule MF_01162

PRO_1000137885

Regions

Transmembrane

258 – 277

20

Helical; Potential

Transmembrane

409 – 433

25

Helical; Potential

Region

15 – 138

124

Acyltransferase HAMAP-Rule MF_01162

Region

233 – 646

414

AMP-binding HAMAP-Rule MF_01162

Sites

Active site

36

1

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

B7MLI2 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: E050AF0C2EFA93BD
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FASTA

719

80,826

        10         20         30         40         50         60 
MLFSFFRNLC RVLYRVRVTG DTKALKGERV LITPNHVSFI DGILLALFLP 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 AENIRGEMER DWYDTGDIVR 

       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

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths."
Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.

Denamur E.
PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S88 / ExPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928161 Genomic DNA. Translation: CAR04371.1.
RefSeq	YP_002392761.1. NC_011742.1.
3D structure databases
ProteinModelPortal	B7MLI2.
ModBase	Search...
Protein-protein interaction databases
STRING	585035.ECS88_3131.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR04371; CAR04371; ECS88_3131.
GeneID	7129536.
KEGG	ecz:ECS88_3131.
PATRIC	18413938. VBIEscCol91599_3073.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0318.
HOGENOM	HOG000004907.
KO	K05939.
OMA	ANWVYLE.
ProtClustDB	PRK08043.
Enzyme and pathway databases
BioCyc	ECOL585035:GJWP-3118-MONOMER.
Family and domain databases
HAMAP	MF_01162. Aas.
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR023775. Bifunctional_Aas. IPR002123. Plipid/glycerol_acylTrfase. [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_ECO45

Accession

Primary (citable) accession number: B7MLI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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

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

Family and domain databases

Entry information

Relevant documents