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P31554

- LPTD_ECOLI

UniProt

P31554 - LPTD_ECOLI

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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

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 - 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
Complete GO annotation...

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
Complete GO annotation...

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 25-784.
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.
InParanoidiP31554.
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

        10         20         30         40         50
MKKRIPTLLA TMIATALYSQ QGLAADLASQ CMLGVPSYDR PLVQGDTNDL
60 70 80 90 100
PVTINADHAK GDYPDDAVFT GSVDIMQGNS RLQADEVQLH QKEAPGQPEP
110 120 130 140 150
VRTVDALGNV HYDDNQVILK GPKGWANLNT KDTNVWEGDY QMVGRQGRGK
160 170 180 190 200
ADLMKQRGEN RYTILDNGSF TSCLPGSDTW SVVGSEIIHD REEQVAEIWN
210 220 230 240 250
ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTTNY FEFYLPYYWN
260 270 280 290 300
IAPNMDATIT PHYMHRRGNI MWENEFRYLS QAGAGLMELD YLPSDKVYED
310 320 330 340 350
EHPNDDSSRR WLFYWNHSGV MDQVWRFNVD YTKVSDPSYF NDFDNKYGSS
360 370 380 390 400
TDGYATQKFS VGYAVQNFNA TVSTKQFQVF SEQNTSSYSA EPQLDVNYYQ
410 420 430 440 450
NDVGPFDTRI YGQAVHFVNT RDDMPEATRV HLEPTINLPL SNNWGSINTE
460 470 480 490 500
AKLLATHYQQ TNLDWYNSRN TTKLDESVNR VMPQFKVDGK MVFERDMEML
510 520 530 540 550
APGYTQTLEP RAQYLYVPYR DQSDIYNYDS SLLQSDYSGL FRDRTYGGLD
560 570 580 590 600
RIASANQVTT GVTSRIYDDA AVERFNISVG QIYYFTESRT GDDNITWEND
610 620 630 640 650
DKTGSLVWAG DTYWRISERW GLRGGIQYDT RLDNVATSNS SIEYRRDEDR
660 670 680 690 700
LVQLNYRYAS PEYIQATLPK YYSTAEQYKN GISQVGAVAS WPIADRWSIV
710 720 730 740 750
GAYYYDTNAN KQADSMLGVQ YSSCCYAIRV GYERKLNGWD NDKQHAVYDN
760 770 780
AIGFNIELRG LSSNYGLGTQ EMLRSNILPY QNTL
Length:784
Mass (Da):89,671
Last modified:November 1, 1997 - v2
Checksum:i906EA3FE8F8D3E1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 25-784.
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.
InParanoidi P31554.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 130 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