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P31554 (LPTD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LPS-assembly protein LptD
Alternative name(s):
Organic solvent tolerance protein
Gene names
Name:lptD
Synonyms:imp, ostA, yabG
Ordered Locus Names:b0054, JW0053
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.16 Ref.17

Subunit structure

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. Ref.11 Ref.12 Ref.17 Ref.19 Ref.20 Ref.21

Subcellular location

Cell outer membrane Ref.6 Ref.9 Ref.11 Ref.14.

Induction

Constitutively expressed. Ref.10

Domain

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. Ref.17 Ref.19 Ref.21

Post-translational modification

Contains two intramolecular disulfide bonds. At least one disulfide bond is required for activity, and protein is probably fully oxidized in vivo. HAMAP-Rule MF_01411

Disruption phenotype

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. Ref.7 Ref.9

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 (Ref.15, Ref.18, Ref.19, Ref.20, Ref.23, Ref.24). BepA can also promote degradation of incorrectly folded LptD (Ref.24).

Sequence similarities

Belongs to the LptD family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.5 Ref.6
Chain25 – 784760LPS-assembly protein LptD HAMAP-Rule MF_01411
PRO_0000020276

Amino acid modifications

Disulfide bond31 ↔ 724 Ref.9 Ref.15 Ref.18 Ref.22
Disulfide bond173 ↔ 725 Ref.9 Ref.15 Ref.18 Ref.22

Experimental info

Mutagenesis529 – 53810Missing: Impairs assembly of the LptD/LptE complex. Does not form native disulfide bonds. Severely compromises outer membrane integrity. Ref.19

Sequences

Sequence LengthMass (Da)Tools
P31554 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 906EA3FE8F8D3E1E

FASTA78489,671
        10         20         30         40         50         60 
MKKRIPTLLA TMIATALYSQ QGLAADLASQ CMLGVPSYDR PLVQGDTNDL PVTINADHAK 

        70         80         90        100        110        120 
GDYPDDAVFT GSVDIMQGNS RLQADEVQLH QKEAPGQPEP VRTVDALGNV HYDDNQVILK 

       130        140        150        160        170        180 
GPKGWANLNT KDTNVWEGDY QMVGRQGRGK ADLMKQRGEN RYTILDNGSF TSCLPGSDTW 

       190        200        210        220        230        240 
SVVGSEIIHD REEQVAEIWN ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTTNY 

       250        260        270        280        290        300 
FEFYLPYYWN IAPNMDATIT PHYMHRRGNI MWENEFRYLS QAGAGLMELD YLPSDKVYED 

       310        320        330        340        350        360 
EHPNDDSSRR WLFYWNHSGV MDQVWRFNVD YTKVSDPSYF NDFDNKYGSS TDGYATQKFS 

       370        380        390        400        410        420 
VGYAVQNFNA TVSTKQFQVF SEQNTSSYSA EPQLDVNYYQ NDVGPFDTRI YGQAVHFVNT 

       430        440        450        460        470        480 
RDDMPEATRV HLEPTINLPL SNNWGSINTE AKLLATHYQQ TNLDWYNSRN TTKLDESVNR 

       490        500        510        520        530        540 
VMPQFKVDGK MVFERDMEML APGYTQTLEP RAQYLYVPYR DQSDIYNYDS SLLQSDYSGL 

       550        560        570        580        590        600 
FRDRTYGGLD RIASANQVTT GVTSRIYDDA AVERFNISVG QIYYFTESRT GDDNITWEND 

       610        620        630        640        650        660 
DKTGSLVWAG DTYWRISERW GLRGGIQYDT RLDNVATSNS SIEYRRDEDR LVQLNYRYAS 

       670        680        690        700        710        720 
PEYIQATLPK YYSTAEQYKN GISQVGAVAS WPIADRWSIV GAYYYDTNAN KQADSMLGVQ 

       730        740        750        760        770        780 
YSSCCYAIRV GYERKLNGWD NDKQHAVYDN AIGFNIELRG LSSNYGLGTQ EMLRSNILPY 


QNTL 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
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]"Role for Skp in LptD assembly in Escherichia coli."
Schwalm J., Mahoney T.F., Soltes G.R., Silhavy T.J.
J. Bacteriol. 195:3734-3742(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB013134 Genomic DNA. Translation: BAA34130.1.
U00096 Genomic DNA. Translation: AAC73165.1.
AP009048 Genomic DNA. Translation: BAB96622.1.
PIRF64726.
RefSeqNP_414596.1. NC_000913.3.
YP_488360.1. NC_007779.1.

3D structure databases

ProteinModelPortalP31554.
SMRP31554. Positions 49-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10029N.
IntActP31554. 8 interactions.
MINTMINT-1293333.
STRING511145.b0054.

Protein family/group databases

TCDB1.B.42.1.2. the outer membrane lipopolysaccharide export porin (lps-ep) family.

2D gel databases

SWISS-2DPAGEP31554.

Proteomic databases

PaxDbP31554.
PRIDEP31554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73165; AAC73165; b0054.
BAB96622; BAB96622; BAB96622.
GeneID12930729.
945011.
KEGGecj:Y75_p0054.
eco:b0054.
PATRIC32115207. VBIEscCol129921_0055.

Organism-specific databases

EchoBASEEB1529.
EcoGeneEG11569. lptD.

Phylogenomic databases

eggNOGCOG1452.
HOGENOMHOG000218450.
KOK04744.
OMADYSHLDW.
OrthoDBEOG6SZ1CP.
PhylomeDBP31554.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP31554.

Family and domain databases

HAMAPMF_01411. LPS_assembly_LptD.
InterProIPR020889. LipoPS_assembly_LptD.
IPR005653. OstA-like_N.
IPR007543. OstA_C.
[Graphical view]
PfamPF03968. OstA. 1 hit.
PF04453. OstA_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP31554.

Entry information

Entry nameLPTD_ECOLI
AccessionPrimary (citable) accession number: P31554
Secondary accession number(s): P75631
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene