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Protein

Octanoyltransferase

Gene

lipB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.UniRule annotation2 Publications

Miscellaneous

In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.

Catalytic activityi

Octanoyl-[acyl-carrier-protein] + protein = protein N6-(octanoyl)lysine + [acyl-carrier-protein].UniRule annotation

Kineticsi

  1. KM=10.2 µM for octanoyl-ACP1 Publication
  2. KM=13.2 µM for apo-H protein1 Publication

    pH dependencei

    Optimum pH is about 7.5.1 Publication

    Pathwayi: protein lipoylation via endogenous pathway

    This protein is involved in step 1 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Octanoyltransferase (lipB)
    2. Lipoyl synthase (lipA)
    This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei135Lowers pKa of active site CysUniRule annotation1
    Active sitei169Acyl-thioester intermediate1

    GO - Molecular functioni

    • catalytic activity Source: EcoliWiki
    • lipoyl(octanoyl) transferase activity Source: EcoCyc
    • octanoyltransferase activity Source: EcoCyc
    • octanoyl transferase activity (acting on glycine-cleavage complex H protein) Source: UniProtKB-EC
    • transferase activity Source: EcoliWiki

    GO - Biological processi

    • cellular protein modification process Source: EcoliWiki
    • lipoate biosynthetic process Source: EcoliWiki
    • lipoate metabolic process Source: EcoliWiki
    • negative regulation of gene expression Source: EcoliWiki
    • protein lipoylation Source: GO_Central

    Keywordsi

    Molecular functionAcyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11591-MONOMER
    MetaCyc:EG11591-MONOMER
    UniPathwayiUPA00538; UER00592

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    OctanoyltransferaseUniRule annotation (EC:2.3.1.181UniRule annotation)
    Alternative name(s):
    Lipoate-protein ligase BUniRule annotation
    Lipoyl/octanoyl transferaseUniRule annotation
    Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferaseUniRule annotation
    Gene namesi
    Name:lipBUniRule annotation
    Ordered Locus Names:b0630, JW5089
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11591 lipB

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi137C → A: No effect on activity. 1
    Mutagenesisi147C → A: No effect on activity. 1
    Mutagenesisi169C → A: 1% of wild-type activity. 1 Publication1
    Mutagenesisi169C → S: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000628341 – 213OctanoyltransferaseAdd BLAST213

    Proteomic databases

    PaxDbiP60720
    PRIDEiP60720

    Interactioni

    Subunit structurei

    Monomer or homotrimer. Both forms are active.1 Publication

    Protein-protein interaction databases

    BioGridi4261534, 35 interactors
    STRINGi316385.ECDH10B_0699

    Structurei

    3D structure databases

    ProteinModelPortaliP60720
    SMRiP60720
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini32 – 207BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST176

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni71 – 78Substrate bindingUniRule annotation8
    Regioni138 – 140Substrate bindingUniRule annotation3
    Regioni151 – 153Substrate bindingUniRule annotation3

    Sequence similaritiesi

    Belongs to the LipB family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4108BDP Bacteria
    COG0321 LUCA
    HOGENOMiHOG000194321
    InParanoidiP60720
    KOiK03801
    OMAiMHGFAFN
    PhylomeDBiP60720

    Family and domain databases

    CDDicd16444 LipB, 1 hit
    HAMAPiMF_00013 LipB, 1 hit
    InterProiView protein in InterPro
    IPR004143 BPL_LPL_catalytic
    IPR000544 Octanoyltransferase
    IPR020605 Octanoyltransferase_CS
    PfamiView protein in Pfam
    PF03099 BPL_LplA_LipB, 1 hit
    PIRSFiPIRSF016262 LPLase, 1 hit
    TIGRFAMsiTIGR00214 lipB, 1 hit
    PROSITEiView protein in PROSITE
    PS51733 BPL_LPL_CATALYTIC, 1 hit
    PS01313 LIPB, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P60720-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MYQDKILVRQ LGLQPYEPIS QAMHEFTDTR DDSTLDEIWL VEHYPVFTQG
    60 70 80 90 100
    QAGKAEHILM PGDIPVIQSD RGGQVTYHGP GQQVMYVLLN LKRRKLGVRE
    110 120 130 140 150
    LVTLLEQTVV NTLAELGIEA HPRADAPGVY VGEKKICSLG LRIRRGCSFH
    160 170 180 190 200
    GLALNVNMDL SPFLRINPCG YAGMEMAKIS QWKPEATTNN IAPRLLENIL
    210
    ALLNNPDFEY ITA
    Length:213
    Mass (Da):23,883
    Last modified:April 13, 2004 - v1
    Checksum:i56EE2BB105F99EAD
    GO

    Sequence cautioni

    The sequence AAA66342 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAB40830 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti33S → D in AAA66342 (PubMed:8444795).Curated1

    Mass spectrometryi

    Molecular mass is 23880.45±1.31 Da from positions 1 - 213. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L07636 Genomic DNA Translation: AAA66342.1 Different initiation.
    U82598 Genomic DNA Translation: AAB40830.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73731.2
    AP009048 Genomic DNA Translation: BAA35273.2
    PIRiD64797
    RefSeqiNP_415163.2, NC_000913.3
    WP_000284027.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC73731; AAC73731; b0630
    BAA35273; BAA35273; BAA35273
    GeneIDi945217
    KEGGiecj:JW5089
    eco:b0630
    PATRICifig|1411691.4.peg.1638

    Similar proteinsi

    Entry informationi

    Entry nameiLIPB_ECOLI
    AccessioniPrimary (citable) accession number: P60720
    Secondary accession number(s): P30976, P77684, Q8XBQ2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: March 28, 2018
    This is version 113 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

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