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P31554

- LPTD_ECOLI

UniProt

P31554 - LPTD_ECOLI

Protein

LPS-assembly protein LptD

Gene

lptD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance.8 PublicationsUniRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. Gram-negative-bacterium-type cell outer membrane assembly Source: EcoCyc
    2. lipopolysaccharide transport Source: EcoliWiki
    3. response to organic substance Source: EcoCyc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11569-MONOMER.
    ECOL316407:JW0053-MONOMER.
    MetaCyc:EG11569-MONOMER.

    Protein family/group databases

    TCDBi1.B.42.1.2. the outer membrane lipopolysaccharide export porin (lps-ep) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LPS-assembly protein LptDUniRule annotation
    Alternative name(s):
    Organic solvent tolerance protein
    Gene namesi
    Name:lptDUniRule annotation
    Synonyms:imp, ostA, yabG
    Ordered Locus Names:b0054, JW0053
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11569. lptD.

    Subcellular locationi

    Cell outer membrane 4 PublicationsUniRule annotation

    GO - Cellular componenti

    1. cell outer membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mutations alter the permeability of the outer membrane resulting in increased sensitivity to detergents, antibiotics and dyes. Depletion leads to filamentation followed by membrane rupture and cell lysis.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi529 – 53810Missing: Impairs assembly of the LptD/LptE complex. Does not form native disulfide bonds. Severely compromises outer membrane integrity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24242 PublicationsUniRule annotationAdd
    BLAST
    Chaini25 – 784760LPS-assembly protein LptDPRO_0000020276Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 724
    Disulfide bondi173 ↔ 725

    Post-translational modificationi

    Contains two intramolecular disulfide bonds. At least one disulfide bond is required for activity, and protein is probably fully oxidized in vivo.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP31554.
    PRIDEiP31554.

    2D gel databases

    SWISS-2DPAGEP31554.

    Expressioni

    Inductioni

    Constitutively expressed.1 Publication

    Gene expression databases

    GenevestigatoriP31554.

    Interactioni

    Subunit structurei

    Component of the lipopolysaccharide transport and assembly complex. Interacts with LptE and LptA. May interact with LptE during assembly of LptD by the beta-barrel assembly machine.6 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    lptAP0ADV13EBI-549369,EBI-1132001
    lptEP0ADC13EBI-549369,EBI-1119442

    Protein-protein interaction databases

    DIPiDIP-10029N.
    IntActiP31554. 8 interactions.
    MINTiMINT-1293333.
    STRINGi511145.b0054.

    Structurei

    3D structure databases

    ProteinModelPortaliP31554.
    SMRiP31554. Positions 49-96.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Contains an N-terminal soluble domain that is likely periplasmic and interacts with LptA, and a C-terminal transmembrane domain, which is predicted to be a beta-barrel and interacts with LptE. Residues 529-538 play a key role in interaction with LptE.3 Publications

    Sequence similaritiesi

    Belongs to the LptD family.UniRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1452.
    HOGENOMiHOG000218450.
    KOiK04744.
    OMAiDYSHLDW.
    OrthoDBiEOG6SZ1CP.
    PhylomeDBiP31554.

    Family and domain databases

    HAMAPiMF_01411. LPS_assembly_LptD.
    InterProiIPR020889. LipoPS_assembly_LptD.
    IPR005653. OstA-like_N.
    IPR007543. OstA_C.
    [Graphical view]
    PfamiPF03968. OstA. 1 hit.
    PF04453. OstA_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31554-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKRIPTLLA TMIATALYSQ QGLAADLASQ CMLGVPSYDR PLVQGDTNDL    50
    PVTINADHAK GDYPDDAVFT GSVDIMQGNS RLQADEVQLH QKEAPGQPEP 100
    VRTVDALGNV HYDDNQVILK GPKGWANLNT KDTNVWEGDY QMVGRQGRGK 150
    ADLMKQRGEN RYTILDNGSF TSCLPGSDTW SVVGSEIIHD REEQVAEIWN 200
    ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTTNY FEFYLPYYWN 250
    IAPNMDATIT PHYMHRRGNI MWENEFRYLS QAGAGLMELD YLPSDKVYED 300
    EHPNDDSSRR WLFYWNHSGV MDQVWRFNVD YTKVSDPSYF NDFDNKYGSS 350
    TDGYATQKFS VGYAVQNFNA TVSTKQFQVF SEQNTSSYSA EPQLDVNYYQ 400
    NDVGPFDTRI YGQAVHFVNT RDDMPEATRV HLEPTINLPL SNNWGSINTE 450
    AKLLATHYQQ TNLDWYNSRN TTKLDESVNR VMPQFKVDGK MVFERDMEML 500
    APGYTQTLEP RAQYLYVPYR DQSDIYNYDS SLLQSDYSGL FRDRTYGGLD 550
    RIASANQVTT GVTSRIYDDA AVERFNISVG QIYYFTESRT GDDNITWEND 600
    DKTGSLVWAG DTYWRISERW GLRGGIQYDT RLDNVATSNS SIEYRRDEDR 650
    LVQLNYRYAS PEYIQATLPK YYSTAEQYKN GISQVGAVAS WPIADRWSIV 700
    GAYYYDTNAN KQADSMLGVQ YSSCCYAIRV GYERKLNGWD NDKQHAVYDN 750
    AIGFNIELRG LSSNYGLGTQ EMLRSNILPY QNTL 784
    Length:784
    Mass (Da):89,671
    Last modified:November 1, 1997 - v2
    Checksum:i906EA3FE8F8D3E1E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB013134 Genomic DNA. Translation: BAA34130.1.
    U00096 Genomic DNA. Translation: AAC73165.1.
    AP009048 Genomic DNA. Translation: BAB96622.1.
    PIRiF64726.
    RefSeqiNP_414596.1. NC_000913.3.
    YP_488360.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73165; AAC73165; b0054.
    BAB96622; BAB96622; BAB96622.
    GeneIDi12930729.
    945011.
    KEGGiecj:Y75_p0054.
    eco:b0054.
    PATRICi32115207. VBIEscCol129921_0055.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB013134 Genomic DNA. Translation: BAA34130.1 .
    U00096 Genomic DNA. Translation: AAC73165.1 .
    AP009048 Genomic DNA. Translation: BAB96622.1 .
    PIRi F64726.
    RefSeqi NP_414596.1. NC_000913.3.
    YP_488360.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P31554.
    SMRi P31554. Positions 49-96.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10029N.
    IntActi P31554. 8 interactions.
    MINTi MINT-1293333.
    STRINGi 511145.b0054.

    Protein family/group databases

    TCDBi 1.B.42.1.2. the outer membrane lipopolysaccharide export porin (lps-ep) family.

    2D gel databases

    SWISS-2DPAGE P31554.

    Proteomic databases

    PaxDbi P31554.
    PRIDEi P31554.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73165 ; AAC73165 ; b0054 .
    BAB96622 ; BAB96622 ; BAB96622 .
    GeneIDi 12930729.
    945011.
    KEGGi ecj:Y75_p0054.
    eco:b0054.
    PATRICi 32115207. VBIEscCol129921_0055.

    Organism-specific databases

    EchoBASEi EB1529.
    EcoGenei EG11569. lptD.

    Phylogenomic databases

    eggNOGi COG1452.
    HOGENOMi HOG000218450.
    KOi K04744.
    OMAi DYSHLDW.
    OrthoDBi EOG6SZ1CP.
    PhylomeDBi P31554.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11569-MONOMER.
    ECOL316407:JW0053-MONOMER.
    MetaCyc:EG11569-MONOMER.

    Miscellaneous databases

    PROi P31554.

    Gene expression databases

    Genevestigatori P31554.

    Family and domain databases

    HAMAPi MF_01411. LPS_assembly_LptD.
    InterProi IPR020889. LipoPS_assembly_LptD.
    IPR005653. OstA-like_N.
    IPR007543. OstA_C.
    [Graphical view ]
    Pfami PF03968. OstA. 1 hit.
    PF04453. OstA_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "N-hexane sensitivity of Escherichia coli due to low expression of ostA/imp by insertion of IS2 and identification of the gene product as an outer membrane protein."
      Abe S., Okutsu T., Negishi T., Nakajima H., Aono R.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-29.
      Strain: K12 / EMG2.
    6. "N-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA encoding an 87 kDa minor protein associated with the outer membrane."
      Abe S., Okutsu T., Nakajima H., Kakuda N., Ohtsu I., Aono R.
      Microbiology 149:1265-1273(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-32, SUBCELLULAR LOCATION, FUNCTION IN HEXANE RESISTANCE.
      Strain: K12 / JA300 / ATCC 33588 / DSM 4776 / NCIMB 12220.
    7. "Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability."
      Sampson B.A., Misra R., Benson S.A.
      Genetics 122:491-501(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Cloning of organic solvent tolerance gene ostA that determines n-hexane tolerance level in Escherichia coli."
      Aono R., Negishi T., Nakajima H.
      Appl. Environ. Microbiol. 60:4624-4626(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HEXANE RESISTANCE.
      Strain: K12 / JA300 / ATCC 33588 / DSM 4776 / NCIMB 12220.
    9. "Imp/OstA is required for cell envelope biogenesis in Escherichia coli."
      Braun M., Silhavy T.J.
      Mol. Microbiol. 45:1289-1302(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DISULFIDE BONDS.
    10. "Transcriptional analysis of the ostA/imp gene involved in organic solvent sensitivity in Escherichia coli."
      Ohtsu I., Kakuda N., Tsukagoshi N., Dokyu N., Takagi H., Wachi M., Aono R.
      Biosci. Biotechnol. Biochem. 68:458-461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    12. "Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli."
      Wu T., McCandlish A.C., Gronenberg L.S., Chng S.-S., Silhavy T.J., Kahne D.
      Proc. Natl. Acad. Sci. U.S.A. 103:11754-11759(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH LPTE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    13. "Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli."
      Sperandeo P., Lau F.K., Carpentieri A., De Castro C., Molinaro A., Deho G., Silhavy T.J., Polissi A.
      J. Bacteriol. 190:4460-4469(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GENE NAME.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    14. "Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex."
      Chng S.S., Gronenberg L.S., Kahne D.
      Biochemistry 49:4565-4567(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential beta-barrel protein LptD."
      Denoncin K., Vertommen D., Paek E., Collet J.F.
      J. Biol. Chem. 285:29425-29433(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS, ASSEMBLY.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    16. "The properties of the outer membrane localized Lipid A transporter LptD."
      Haarmann R., Ibrahim M., Stevanovic M., Bredemeier R., Schleiff E.
      J. Phys. Condens. Matter. 22:454124-454124(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane."
      Chng S.S., Ruiz N., Chimalakonda G., Silhavy T.J., Kahne D.
      Proc. Natl. Acad. Sci. U.S.A. 107:5363-5368(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LPTE, DOMAIN.
    18. "Nonconsecutive disulfide bond formation in an essential integral outer membrane protein."
      Ruiz N., Chng S.S., Hiniker A., Kahne D., Silhavy T.J.
      Proc. Natl. Acad. Sci. U.S.A. 107:12245-12250(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    19. "The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel."
      Freinkman E., Chng S.S., Kahne D.
      Proc. Natl. Acad. Sci. U.S.A. 108:2486-2491(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPTE, DOMAIN, MUTAGENESIS OF 529-ASP--SER-538.
    20. "Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli."
      Chimalakonda G., Ruiz N., Chng S.S., Garner R.A., Kahne D., Silhavy T.J.
      Proc. Natl. Acad. Sci. U.S.A. 108:2492-2497(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPTE.
    21. "Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export."
      Freinkman E., Okuda S., Ruiz N., Kahne D.
      Biochemistry 51:4800-4806(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPTA, DOMAIN.
    22. "Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export."
      Chng S.S., Xue M., Garner R.A., Kadokura H., Boyd D., Beckwith J., Kahne D.
      Science 337:1665-1668(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    23. Cited for: ASSEMBLY.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    24. "Protease homolog BepA (YfgC) promotes assembly and degradation of beta-barrel membrane proteins in Escherichia coli."
      Narita S., Masui C., Suzuki T., Dohmae N., Akiyama Y.
      Proc. Natl. Acad. Sci. U.S.A. 110:E3612-E3621(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSEMBLY.
      Strain: K12.

    Entry informationi

    Entry nameiLPTD_ECOLI
    AccessioniPrimary (citable) accession number: P31554
    Secondary accession number(s): P75631
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The correct assembly of LptD depends on the thiol:disulfide interchange proteins DsbA and DsbC, the chaperone proteins SurA and Skp, LptE and the chaperone/protease BepA (PubMed:20615876, PubMed:20566849, PubMed:21257904, PubMed:21257909, PubMed:23772069, PubMed:24003122). BepA can also promote degradation of incorrectly folded LptD (PubMed:24003122).6 Publications

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3