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Protein

Tol-Pal system protein TolR

Gene

tolR

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

Functioni

Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:1683466, PubMed:17233825). Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction (PubMed:11722743). Is also involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA (PubMed:1683466, PubMed:3294803). The Tol-Pal system is also required for polar localization of chemoreceptors clusters (PubMed:24720726).1 Publication5 Publications

GO - Molecular functioni

GO - Biological processi

  • bacteriocin transport Source: EcoliWiki
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • protein transport Source: InterPro

Keywordsi

Biological processCell cycle, Cell division

Enzyme and pathway databases

BioCyciEcoCyc:EG11011-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Tol-Pal system protein TolRUniRule annotationCurated
Gene namesi
Name:tolR1 PublicationUniRule annotation
Ordered Locus Names:b0738, JW0728
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11011 tolR

Subcellular locationi

  • Cell inner membrane UniRule annotation2 Publications; Single-pass membrane protein UniRule annotation1 Publication1 Publication
  • Note: Accumulates at cell constriction sites. Recruitment to the division site is dependent on FtsN activity.1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 17Cytoplasmic2 PublicationsAdd BLAST17
Transmembranei18 – 38HelicalUniRule annotationAdd BLAST21
Topological domaini39 – 142Periplasmic1 Publication1 PublicationAdd BLAST104

GO - Cellular componenti

  • cell division site Source: EcoCyc
  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoliWiki

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutants lacking the tol-pal cluster suffer delayed outer membrane invagination and contain large outer membrane blebs at constriction sites and cell poles.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23D → A: Decreases TolA-Pal interaction. 1 Publication1
Mutagenesisi23D → E: No change in TolA-Pal interaction. 1 Publication1
Mutagenesisi23D → R: Abolishes TolA-Pal interaction. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001291401 – 142Tol-Pal system protein TolRAdd BLAST142

Proteomic databases

PaxDbiP0ABV6
PRIDEiP0ABV6

Interactioni

Subunit structurei

The Tol-Pal system is composed of five core proteins: the inner membrane proteins TolA, TolQ and TolR, the periplasmic protein TolB and the outer membrane protein Pal. They form a network linking the inner and outer membranes and the peptidoglycan layer (PubMed:17233825). TolR forms homodimers (PubMed:10419942, PubMed:26354441). Interacts with the N-terminal domain of TolA and with TolQ (PubMed:7744737, PubMed:10419942).1 Publication3 Publications

Protein-protein interaction databases

BioGridi4261829, 235 interactors
DIPiDIP-48143N
IntActiP0ABV6, 3 interactors
STRINGi316385.ECDH10B_0805

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi52 – 57Combined sources6
Beta strandi64 – 68Combined sources5
Beta strandi74 – 78Combined sources5
Beta strandi81 – 86Combined sources6
Helixi88 – 101Combined sources14
Beta strandi107 – 111Combined sources5
Helixi117 – 129Combined sources13
Beta strandi136 – 139Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5BY4X-ray1.70A36-142[»]
ProteinModelPortaliP0ABV6
SMRiP0ABV6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal transmembrane domain is involved in interaction with TolA and TolQ, while the central and C-terminal domains are involved in dimerization. The C-terminal domain is also involved in interaction with TolA and in association with the membranes (PubMed:10419942). May undergo large scale structural remodeling, where the N- and C-terminal sequences unfold in order for the protein to both reach and bind the peptidoglycan layer around 90 angstroem away from the inner membrane (PubMed:26354441).2 Publications

Sequence similaritiesi

Belongs to the ExbD/TolR family.UniRule annotationCurated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0848 LUCA
HOGENOMiHOG000134906
InParanoidiP0ABV6
KOiK03560
OMAiMMTHGVK
PhylomeDBiP0ABV6

Family and domain databases

HAMAPiMF_02203 TolR, 1 hit
InterProiView protein in InterPro
IPR003400 ExbD
IPR014168 Tol-Pal_TolR
PANTHERiPTHR30558 PTHR30558, 1 hit
PfamiView protein in Pfam
PF02472 ExbD, 1 hit
TIGRFAMsiTIGR02801 tolR, 1 hit

Sequencei

Sequence statusi: Complete.

P0ABV6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARARGRGRR DLKSEINIVP LLDVLLVLLL IFMATAPIIT QSVEVDLPDA
60 70 80 90 100
TESQAVSSND NPPVIVEVSG IGQYTVVVEK DRLERLPPEQ VVAEVSSRFK
110 120 130 140
ANPKTVFLIG GAKDVPYDEI IKALNLLHSA GVKSVGLMTQ PI
Length:142
Mass (Da):15,383
Last modified:October 25, 2005 - v1
Checksum:i936FE0033172600B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16489 Genomic DNA Translation: AAA83921.1
U00096 Genomic DNA Translation: AAC73832.1
AP009048 Genomic DNA Translation: BAA35404.1
PIRiC25980 BVECTR
RefSeqiNP_415266.1, NC_000913.3
WP_000090097.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73832; AAC73832; b0738
BAA35404; BAA35404; BAA35404
GeneIDi945328
KEGGiecj:JW0728
eco:b0738
PATRICifig|1411691.4.peg.1534

Similar proteinsi

Entry informationi

Entry nameiTOLR_ECOLI
AccessioniPrimary (citable) accession number: P0ABV6
Secondary accession number(s): P05829
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: May 23, 2018
This is version 95 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, Reference proteome

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