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Protein

Lipopolysaccharide export system protein LptA

Gene

lptA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm.UniRule annotation5 Publications

GO - Molecular functioni

  • glycolipid transporter activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • lipopolysaccharide binding Source: InterPro

GO - Biological processi

  • lipopolysaccharide transport Source: EcoCyc

Keywordsi

Biological processTransport

Enzyme and pathway databases

BioCyciEcoCyc:YHBN-MONOMER
MetaCyc:YHBN-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:
Lipopolysaccharide export system protein LptAUniRule annotation
Gene namesi
Name:lptAUniRule annotation
Synonyms:yhbN
Ordered Locus Names:b3200, JW3167
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12618 lptA

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Results in an earlier growth arrest and onset of cell lethality.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36I → D or E: No change in activity. 1 Publication1
Mutagenesisi38I → D: Decrease in activity. 1 Publication1
Mutagenesisi38I → E: No change in activity. 1 Publication1
Mutagenesisi76R → D or E: No change in activity. 1 Publication1
Mutagenesisi95F → A: No change in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27UniRule annotation1 PublicationAdd BLAST27
ChainiPRO_000001391428 – 185Lipopolysaccharide export system protein LptAAdd BLAST158

Proteomic databases

EPDiP0ADV1
PaxDbiP0ADV1
PRIDEiP0ADV1

Expressioni

Inductioni

Transcriptionally regulated by sigma-E factor.1 Publication

Interactioni

Subunit structurei

Component of the lipopolysaccharide transport and assembly complex. Can form head-to-tail homodimers and oligomers. Interacts with LptC, LptD and with the lipid A domain of LPS.UniRule annotation7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259280249 interactors.
DIPiDIP-12262N
IntActiP0ADV1 5 interactors.
STRINGi316385.ECDH10B_3374

Structurei

Secondary structure

1185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 33Combined sources5
Beta strandi36 – 46Combined sources11
Turni47 – 50Combined sources4
Beta strandi51 – 62Combined sources12
Beta strandi65 – 75Combined sources11
Beta strandi85 – 89Combined sources5
Beta strandi94 – 97Combined sources4
Beta strandi105 – 108Combined sources4
Beta strandi110 – 115Combined sources6
Helixi116 – 118Combined sources3
Beta strandi120 – 131Combined sources12
Beta strandi134 – 144Combined sources11
Turni145 – 148Combined sources4
Beta strandi149 – 153Combined sources5
Beta strandi155 – 157Combined sources3
Beta strandi160 – 162Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R19X-ray2.16A/B27-185[»]
2R1AX-ray3.26A/B/C/D/E/F/G/H27-185[»]
ProteinModelPortaliP0ADV1
SMRiP0ADV1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADV1

Family & Domainsi

Domaini

The N-terminal domain interacts with LptC, at the inner membrane, and the C-terminal domain interacts with LptD, at the outer membrane.1 Publication

Sequence similaritiesi

Belongs to the LptA family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105WI0 Bacteria
COG1934 LUCA
HOGENOMiHOG000264762
InParanoidiP0ADV1
KOiK09774
OMAiRADRDKP
PhylomeDBiP0ADV1

Family and domain databases

HAMAPiMF_01914 LPS_assembly_LptA, 1 hit
InterProiView protein in InterPro
IPR014340 LptA
IPR005653 OstA-like_N
PfamiView protein in Pfam
PF03968 OstA, 1 hit
TIGRFAMsiTIGR03002 outer_YhbN_LptA, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0ADV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFKTNKLSL NLVLASSLLA ASIPAFAVTG DTDQPIHIES DQQSLDMQGN
60 70 80 90 100
VVTFTGNVIV TQGTIKINAD KVVVTRPGGE QGKEVIDGYG KPATFYQMQD
110 120 130 140 150
NGKPVEGHAS QMHYELAKDF VVLTGNAYLQ QVDSNIKGDK ITYLVKEQKM
160 170 180
QAFSDKGKRV TTVLVPSQLQ DKNNKGQTPA QKKGN
Length:185
Mass (Da):20,127
Last modified:December 6, 2005 - v1
Checksum:iBA69198479C68DC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12684 Genomic DNA Translation: AAB60161.1
U18997 Genomic DNA Translation: AAA58002.1
U00096 Genomic DNA Translation: AAC76232.1
AP009048 Genomic DNA Translation: BAE77244.1
PIRiB65111
RefSeqiNP_417667.1, NC_000913.3
WP_000669785.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76232; AAC76232; b3200
BAE77244; BAE77244; BAE77244
GeneIDi947920
KEGGiecj:JW3167
eco:b3200
PATRICifig|1411691.4.peg.3531

Similar proteinsi

Entry informationi

Entry nameiLPTA_ECOLI
AccessioniPrimary (citable) accession number: P0ADV1
Secondary accession number(s): P38685, Q2M912
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: March 28, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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