P0ADV1 (LPTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lipopolysaccharide export system protein lptA | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 185 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Required for the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. May act as a chaperone that facilitates LPS transfer across the aquaeous environment of the periplasm. Interacts specifically with the lipid A domain of LPS. Ref.5 Ref.6 Ref.7 Ref.8 |
| Subunit structure | |
| Subcellular location | |
| Induction | Transcriptionally regulated by sigma-E factor. Ref.6 |
| Disruption phenotype | Results in an earlier growth arrest and onset of cell lethality. Ref.5 |
| Sequence similarities | Belongs to the lptA family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Periplasm |
| Domain | Signal |
| Molecular function | Chaperone |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | lipopolysaccharide transport Inferred from mutant phenotype Ref.6. Source: EcoCyc |
| Cellular component | periplasmic space Inferred from direct assay Ref.6. Source: EcoCyc |
| Molecular function | glycolipid transporter activity Inferred from mutant phenotype Ref.6. Source: EcoCyc lipopolysaccharide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | Ref.4 | |||||||||||||||||||||||||||||||
| Chain | 28 – 185 | 158 | Lipopolysaccharide export system protein lptA | PRO_0000013914 | ||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||
| Mutagenesis | 36 | 1 | I → D or E: No change in activity. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 38 | 1 | I → D: Decrease in activity. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 38 | 1 | I → E: No change in activity. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 76 | 1 | R → D or E: No change in activity. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 95 | 1 | F → A: No change in activity. Ref.9 | |||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Helix | 29 – 33 | 5 | ||||||||||||||||||||||||||||||||
| Beta strand | 36 – 46 | 11 | ||||||||||||||||||||||||||||||||
| Turn | 47 – 50 | 4 | ||||||||||||||||||||||||||||||||
| Beta strand | 51 – 62 | 12 | ||||||||||||||||||||||||||||||||
| Beta strand | 65 – 75 | 11 | ||||||||||||||||||||||||||||||||
| Beta strand | 85 – 89 | 5 | ||||||||||||||||||||||||||||||||
| Beta strand | 94 – 97 | 4 | ||||||||||||||||||||||||||||||||
| Beta strand | 105 – 108 | 4 | ||||||||||||||||||||||||||||||||
| Beta strand | 110 – 115 | 6 | ||||||||||||||||||||||||||||||||
| Helix | 116 – 118 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 120 – 131 | 12 | ||||||||||||||||||||||||||||||||
| Beta strand | 134 – 144 | 11 | ||||||||||||||||||||||||||||||||
| Turn | 145 – 148 | 4 | ||||||||||||||||||||||||||||||||
| Beta strand | 149 – 153 | 5 | ||||||||||||||||||||||||||||||||
| Beta strand | 155 – 157 | 3 | ||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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: 7876255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [2] | "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 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "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: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-39. Strain: K12 / EMG2. |
| [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: 16765569] [Abstract] Cited for: FUNCTION IN LPS BIOSYNTHESIS, DISRUPTION PHENOTYPE. |
| [6] | "Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli." Sperandeo P., Cescutti R., Villa R., Di Benedetto C., Candia D., Deho G., Polissi A. J. Bacteriol. 189:244-253(2007) [PubMed: 17056748] [Abstract] Cited for: FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT, SUBCELLULAR LOCATION, INDUCTION. |
| [7] | "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: 18424520] [Abstract] Cited for: FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574. |
| [8] | "The LptA protein of Escherichia coli is a periplasmic lipid A-binding protein involved in the lipopolysaccharide export pathway." Tran A.X., Trent M.S., Whitfield C. J. Biol. Chem. 283:20342-20349(2008) [PubMed: 18480051] [Abstract] Cited for: FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT, SUBUNIT, SUBCELLULAR LOCATION, LIPID A-BINDING. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [9] | "Novel structure of the conserved Gram-negative lipopolysaccharide transport protein A and mutagenesis analysis." Suits M.D.L., Sperandeo P., Deho G., Polissi A., Jia Z. J. Mol. Biol. 380:476-488(2008) [PubMed: 18534617] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 27-185, SUBUNIT, MUTAGENESIS OF ILE-36; ILE-38; ARG-76 AND PHE-95. Strain: K12. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U12684 Genomic DNA. Translation: AAB60161.1. U18997 Genomic DNA. Translation: AAA58002.1. U00096 Genomic DNA. Translation: AAC76232.1. AP009048 Genomic DNA. Translation: BAE77244.1. | ||||||||||||||||||
| PIR | B65111. | ||||||||||||||||||
| RefSeq | NP_417667.1. NC_000913.2. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0ADV1. | ||||||||||||||||||
| SMR | P0ADV1. Positions 28-164. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P0ADV1. 3 interactions. | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| TCDB | 1.B.42.1.2. outer membrane lipopolysaccharide export porin (LPS-EP) family. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | EBESCT00000001811; EBESCP00000001811; EBESCG00000001495. EBESCT00000017131; EBESCP00000016422; EBESCG00000016190. | ||||||||||||||||||
| GeneID | 947920. | ||||||||||||||||||
| GenomeReviews | Gene locus JW3167 in contig AP009048_GR. Gene locus b3200 in contig U00096_GR. | ||||||||||||||||||
| KEGG | ecj:JW3167. eco:b3200. | ||||||||||||||||||
| PATRIC | 32121820. VBIEscCol129921_3294. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| EchoBASE | EB2502. | ||||||||||||||||||
| EcoGene | EG12618. lptA. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG1934. | ||||||||||||||||||
| GeneTree | EBGT00050000009111. | ||||||||||||||||||
| HOGENOM | HBG701445. | ||||||||||||||||||
| OMA | VTFTDNV. | ||||||||||||||||||
| PhylomeDB | P0ADV1. | ||||||||||||||||||
| ProtClustDB | PRK10894. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | EcoCyc:YHBN-MONOMER. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| Genevestigator | P0ADV1. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR014340. LipoPS_assembly_LptA. IPR005653. OstA-like_N. [Graphical view] | ||||||||||||||||||
| KO | K09774. | ||||||||||||||||||
| Pfam | PF03968. OstA. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR03002. Outer_YhbN_LptA. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | LPTA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0ADV1 Secondary accession number(s): P38685, Q2M912 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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