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P0ADV9

- LPTC_ECOLI

UniProt

P0ADV9 - LPTC_ECOLI

Protein

Lipopolysaccharide export system protein LptC

Gene

lptC

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 74 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.5 PublicationsUniRule annotation

    GO - Molecular functioni

    1. glycolipid transporter activity Source: EcoCyc
    2. identical protein binding Source: IntAct
    3. lipopolysaccharide transmembrane transporter activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. glycolipid transport Source: GOC
    2. lipopolysaccharide transport Source: EcoCyc

    Enzyme and pathway databases

    BioCyciEcoCyc:G7664-MONOMER.
    ECOL316407:JW3166-MONOMER.
    MetaCyc:G7664-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipopolysaccharide export system protein LptCUniRule annotation
    Gene namesi
    Name:lptCUniRule annotation
    Synonyms:yrbK
    Ordered Locus Names:b3199, JW3166
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12806. lptC.

    Subcellular locationi

    Cell inner membrane 2 PublicationsUniRule annotation; Single-pass membrane protein 2 PublicationsUniRule annotation

    GO - Cellular componenti

    1. integral component of membrane Source: EcoCyc
    2. integral component of plasma membrane Source: EcoCyc
    3. outer membrane-bounded periplasmic space Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Leads to irreversible cell damage, growth arrest and an extreme sensitivity to SDS.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561G → V: Impairs LPS transport. Does not abolish interaction with LptA. 1 Publication
    Mutagenesisi153 – 1531G → R: Impairs LPS transport. Fails to interacts with LptA. 1 Publication
    Mutagenesisi177 – 19115Missing: Fails to interact with LptA. Add
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 191191Lipopolysaccharide export system protein LptCPRO_0000169470Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP0ADV9.

    Interactioni

    Subunit structurei

    Component of the lipopolysaccharide transport and assembly complex. Interacts with LptA and the LptBFG transporter complex. When overexpressed, can form homodimers in vivo.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-1131969,EBI-1131969
    lptAP0ADV13EBI-1131969,EBI-1132001

    Protein-protein interaction databases

    DIPiDIP-12912N.
    IntActiP0ADV9. 3 interactions.
    MINTiMINT-7137017.
    STRINGi511145.b3199.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 634
    Beta strandi65 – 706
    Turni71 – 744
    Beta strandi75 – 806
    Beta strandi82 – 865
    Beta strandi92 – 976
    Beta strandi99 – 1035
    Beta strandi107 – 11913
    Beta strandi121 – 1233
    Beta strandi125 – 13713
    Turni138 – 1403
    Beta strandi142 – 15514
    Beta strandi157 – 16610
    Turni167 – 1704
    Beta strandi171 – 18010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MY2X-ray2.20A23-191[»]
    4B54X-ray2.80A/B24-191[»]
    ProteinModelPortaliP0ADV9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ADV9.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2519HelicalUniRule annotationAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LptC family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3117.
    HOGENOMiHOG000125239.
    KOiK11719.
    OMAiWFTQPVM.
    OrthoDBiEOG6W7212.

    Family and domain databases

    HAMAPiMF_01915. LPS_assembly_LptC.
    InterProiIPR010664. LipoPS_assembly_LptC-rel.
    IPR026265. LptC.
    [Graphical view]
    PfamiPF06835. LptC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028513. LptC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0ADV9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKARRWVII VLSLAVLVMI GINMAEKDDT AQVVVNNNDP TYKSEHTDTL    50
    VYNPEGALSY RLIAQHVEYY SDQAVSWFTQ PVLTTFDKDK IPTWSVKADK 100
    AKLTNDRMLY LYGHVEVNAL VPDSQLRRIT TDNAQINLVT QDVTSEDLVT 150
    LYGTTFNSSG LKMRGNLRSK NAELIEKVRT SYEIQNKQTQ P 191
    Length:191
    Mass (Da):21,703
    Last modified:December 6, 2005 - v1
    Checksum:iF6BAE79EA232CD95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21S → G AA sequence (PubMed:19500581)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18997 Genomic DNA. Translation: AAA58001.1.
    U00096 Genomic DNA. Translation: AAC76231.1.
    AP009048 Genomic DNA. Translation: BAE77243.1.
    U12684 Genomic DNA. No translation available.
    PIRiA65111.
    RefSeqiNP_417666.1. NC_000913.3.
    YP_491384.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76231; AAC76231; b3199.
    BAE77243; BAE77243; BAE77243.
    GeneIDi12930285.
    947722.
    KEGGiecj:Y75_p3119.
    eco:b3199.
    PATRICi32121818. VBIEscCol129921_3293.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18997 Genomic DNA. Translation: AAA58001.1 .
    U00096 Genomic DNA. Translation: AAC76231.1 .
    AP009048 Genomic DNA. Translation: BAE77243.1 .
    U12684 Genomic DNA. No translation available.
    PIRi A65111.
    RefSeqi NP_417666.1. NC_000913.3.
    YP_491384.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MY2 X-ray 2.20 A 23-191 [» ]
    4B54 X-ray 2.80 A/B 24-191 [» ]
    ProteinModelPortali P0ADV9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-12912N.
    IntActi P0ADV9. 3 interactions.
    MINTi MINT-7137017.
    STRINGi 511145.b3199.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76231 ; AAC76231 ; b3199 .
    BAE77243 ; BAE77243 ; BAE77243 .
    GeneIDi 12930285.
    947722.
    KEGGi ecj:Y75_p3119.
    eco:b3199.
    PATRICi 32121818. VBIEscCol129921_3293.

    Organism-specific databases

    EchoBASEi EB2657.
    EcoGenei EG12806. lptC.

    Phylogenomic databases

    eggNOGi COG3117.
    HOGENOMi HOG000125239.
    KOi K11719.
    OMAi WFTQPVM.
    OrthoDBi EOG6W7212.

    Enzyme and pathway databases

    BioCyci EcoCyc:G7664-MONOMER.
    ECOL316407:JW3166-MONOMER.
    MetaCyc:G7664-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ADV9.
    PROi P0ADV9.

    Gene expression databases

    Genevestigatori P0ADV9.

    Family and domain databases

    HAMAPi MF_01915. LPS_assembly_LptC.
    InterProi IPR010664. LipoPS_assembly_LptC-rel.
    IPR026265. LptC.
    [Graphical view ]
    Pfami PF06835. LptC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028513. LptC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "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.
    3. "Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant."
      Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X., Reizer A., Saier M.H. Jr., Reizer J.
      J. Biol. Chem. 270:4822-4839(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-191.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides."
      Narita S., Tokuda H.
      FEBS Lett. 583:2160-2164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-5, INTERACTION WITH LPTBFG.
    5. "Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus."
      Sperandeo P., Pozzi C., Deho G., Polissi A.
      Res. Microbiol. 157:547-558(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LPS BIOSYNTHESIS, DISRUPTION PHENOTYPE.
    6. "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 IN LIPOPOLYSACCHARIDE TRANSPORT, SUBCELLULAR LOCATION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    7. "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: SUBUNIT, INTERACTION WITH LPTBFG.
    8. "Characterization of interactions between LPS transport proteins of the Lpt system."
      Bowyer A., Baardsnes J., Ajamian E., Zhang L., Cygler M.
      Biochem. Biophys. Res. Commun. 404:1093-1098(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LPTA.
    9. "New insights into the Lpt machinery for lipopolysaccharide transport to the cell surface: LptA-LptC interaction and LptA stability as sensors of a properly assembled transenvelope complex."
      Sperandeo P., Villa R., Martorana A.M., Samalikova M., Grandori R., Deho G., Polissi A.
      J. Bacteriol. 193:1042-1053(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH LPTA, MUTAGENESIS OF GLY-56; GLY-153 AND 177-LYS--PRO-191.
    10. "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: SUBUNIT, INTERACTION WITH LPTA.
    11. "Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli."
      Tran A.X., Dong C., Whitfield C.
      J. Biol. Chem. 285:33529-33539(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-191, FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiLPTC_ECOLI
    AccessioniPrimary (citable) accession number: P0ADV9
    Secondary accession number(s): P45397, Q2M913
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Interacts with the LptBFG ABC transporter complex, but does not affect its ATPase activity.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3