Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Octanoyltransferase

Gene

lipB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Catalytic activityi

Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(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
    • 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
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11591-MONOMER.
    ECOL316407:JW5089-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

    Complete GO annotation...

    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. 14 interactors.
    STRINGi511145.b0630.

    Structurei

    3D structure databases

    ProteinModelPortaliP60720.
    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
    Contains 1 BPL/LPL catalytic domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4108BDP. Bacteria.
    COG0321. LUCA.
    HOGENOMiHOG000194321.
    InParanoidiP60720.
    KOiK03801.
    OMAiDEKKVCS.
    PhylomeDBiP60720.

    Family and domain databases

    HAMAPiMF_00013. LipB. 1 hit.
    InterProiIPR004143. BPL_LPL_catalytic.
    IPR000544. Octanoyltransferase.
    IPR020605. Octanoyltransferase_CS.
    [Graphical view]
    PfamiPF03099. BPL_LplA_LipB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016262. LPLase. 1 hit.
    TIGRFAMsiTIGR00214. lipB. 1 hit.
    PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
    PS01313. LIPB. 1 hit.
    [Graphical view]

    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.
    PATRICi32116441. VBIEscCol129921_0660.

    Cross-referencesi

    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.

    3D structure databases

    ProteinModelPortaliP60720.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261534. 14 interactors.
    STRINGi511145.b0630.

    Proteomic databases

    PaxDbiP60720.
    PRIDEiP60720.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73731; AAC73731; b0630.
    BAA35273; BAA35273; BAA35273.
    GeneIDi945217.
    KEGGiecj:JW5089.
    eco:b0630.
    PATRICi32116441. VBIEscCol129921_0660.

    Organism-specific databases

    EchoBASEiEB1283.
    EcoGeneiEG11591. lipB.

    Phylogenomic databases

    eggNOGiENOG4108BDP. Bacteria.
    COG0321. LUCA.
    HOGENOMiHOG000194321.
    InParanoidiP60720.
    KOiK03801.
    OMAiDEKKVCS.
    PhylomeDBiP60720.

    Enzyme and pathway databases

    UniPathwayiUPA00538; UER00592.
    BioCyciEcoCyc:EG11591-MONOMER.
    ECOL316407:JW5089-MONOMER.
    MetaCyc:EG11591-MONOMER.

    Miscellaneous databases

    PROiP60720.

    Family and domain databases

    HAMAPiMF_00013. LipB. 1 hit.
    InterProiIPR004143. BPL_LPL_catalytic.
    IPR000544. Octanoyltransferase.
    IPR020605. Octanoyltransferase_CS.
    [Graphical view]
    PfamiPF03099. BPL_LplA_LipB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016262. LPLase. 1 hit.
    TIGRFAMsiTIGR00214. lipB. 1 hit.
    PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
    PS01313. LIPB. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiLIPB_ECOLI
    AccessioniPrimary (citable) accession number: P60720
    Secondary accession number(s): P30976, P77684, Q8XBQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: November 2, 2016
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.