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B7N768

- AAS_ECOLU

UniProt

B7N768 - AAS_ECOLU

Protein

Bifunctional protein Aas

Gene

aas

Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    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.UniRule annotation

    Catalytic activityi

    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.UniRule annotation
    ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein].UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei36 – 361UniRule annotation

    GO - Molecular functioni

    1. acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-KW
    3. long-chain fatty acid [acyl-carrier-protein] ligase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. fatty acid metabolic process Source: InterPro
    2. phospholipid biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Acyltransferase, Ligase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein AasUniRule annotation
    Including the following 2 domains:
    2-acylglycerophosphoethanolamine acyltransferaseUniRule annotation (EC:2.3.1.40UniRule annotation)
    Alternative name(s):
    2-acyl-GPE acyltransferaseUniRule annotation
    Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferaseUniRule annotation
    Acyl-[acyl-carrier-protein] synthetaseUniRule annotation (EC:6.2.1.20UniRule annotation)
    Alternative name(s):
    Acyl-ACP synthetaseUniRule annotation
    Long-chain-fatty-acid--[acyl-carrier-protein] ligaseUniRule annotation
    Gene namesi
    Name:aasUniRule annotation
    Ordered Locus Names:ECUMN_3163
    OrganismiEscherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
    Taxonomic identifieri585056 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000007097: Chromosome

    Subcellular locationi

    Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 719719Bifunctional protein AasPRO_1000137889Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi585056.ECUMN_3163.

    Structurei

    3D structure databases

    ProteinModelPortaliB7N768.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei258 – 27720HelicalUniRule annotationAdd
    BLAST
    Transmembranei409 – 43325HelicalUniRule annotationAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 138124AcyltransferaseAdd
    BLAST
    Regioni233 – 646414AMP-bindingAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family.UniRule annotation
    In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0318.
    HOGENOMiHOG000004907.
    KOiK05939.
    OMAiANWVYLE.
    OrthoDBiEOG6KHFVG.

    Family and domain databases

    HAMAPiMF_01162. Aas.
    InterProiIPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR023775. Bifunctional_Aas.
    IPR002123. Plipid/glycerol_acylTrfase.
    [Graphical view]
    PfamiPF01553. Acyltransferase. 1 hit.
    PF00501. AMP-binding. 1 hit.
    [Graphical view]
    SMARTiSM00563. PlsC. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B7N768-1 [UniParc]FASTAAdd to Basket

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    MLFSFFRNLC RVLYRVRVTG DTQALKGERV LITPNHVSFI DGILLALFLP    50
    VRPVFAVYTS ISQQWYMRWL KSFIDFVPLD PTQPMAIKHL VRLVEQGRPV 100
    VIFPEGRITT TGSLMKIYDG AGFVAAKSGA TVIPVRIEGA ELTHFSRLKG 150
    LVKRRLFPQI TLHILPPTQV EMPDAPRARD RRKIAGEMLH QIMMEARMAV 200
    RPRETLYESL LSAMYRFGAG KKCVEDVNFT PDSYRKLLTK TLFVGRILEK 250
    YSIEGERIGL MLPNAGISAA VIFGAIARRR IPAMMNYTAG VKGLTSAITA 300
    AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFS 350
    HLLMPRLAQV KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI 400
    ADFTTNDRFM SALPLFHSFG LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL 450
    VYDRSCTVLF GTSTFLGHYA RFANPYDFYR LRYVVAGAEK LQESTKQLWQ 500
    DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM DARLLSVPGI 550
    EEGGRLQLKG PNIMNGYLRV EKPGVLEVPT AENVRGEMER GWYDTGDIVR 600
    FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA 650
    SKGEALVLFT TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG 700
    KPDFVTLKSW VDEAEQHDE 719
    Length:719
    Mass (Da):80,784
    Last modified:February 10, 2009 - v1
    Checksum:iC94ACB1EEFCFCCE2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU928163 Genomic DNA. Translation: CAR14329.1.
    RefSeqiYP_002413849.1. NC_011751.1.

    Genome annotation databases

    EnsemblBacteriaiCAR14329; CAR14329; ECUMN_3163.
    GeneIDi7159025.
    KEGGieum:ECUMN_3163.
    PATRICi18445628. VBIEscCol32010_3345.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU928163 Genomic DNA. Translation: CAR14329.1 .
    RefSeqi YP_002413849.1. NC_011751.1.

    3D structure databases

    ProteinModelPortali B7N768.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 585056.ECUMN_3163.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAR14329 ; CAR14329 ; ECUMN_3163 .
    GeneIDi 7159025.
    KEGGi eum:ECUMN_3163.
    PATRICi 18445628. VBIEscCol32010_3345.

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000004907.
    KOi K05939.
    OMAi ANWVYLE.
    OrthoDBi EOG6KHFVG.

    Family and domain databases

    HAMAPi MF_01162. Aas.
    InterProi IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR023775. Bifunctional_Aas.
    IPR002123. Plipid/glycerol_acylTrfase.
    [Graphical view ]
    Pfami PF01553. Acyltransferase. 1 hit.
    PF00501. AMP-binding. 1 hit.
    [Graphical view ]
    SMARTi SM00563. PlsC. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: UMN026 / ExPEC.

    Entry informationi

    Entry nameiAAS_ECOLU
    AccessioniPrimary (citable) accession number: B7N768
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3