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Protein

Protein TonB

Gene

tonB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847).1 Publication

GO - Molecular functioni

GO - Biological processi

  • cobalamin transport Source: EcoCyc
  • colicin transport Source: EcoCyc
  • protein transport Source: UniProtKB-KW
  • siderophore transport Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Bacteriocin transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11012-MONOMER.
ECOL316407:JW5195-MONOMER.
MetaCyc:EG11012-MONOMER.

Protein family/group databases

TCDBi2.C.1.1.1. the tonb-exbb-exbd/tola-tolq-tolr (tonb) family of auxiliary proteins for energization of outer membrane receptor (omr)-mediated active transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein TonB
Gene namesi
Name:tonB
Synonyms:exbA
Ordered Locus Names:b1252, JW5195
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11012. tonB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 3232Helical; Signal-anchorCuratedAdd
BLAST
Topological domaini33 – 239207Periplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intrinsic component of external side of plasma membrane Source: EcoCyc
  • outer membrane-bounded periplasmic space Source: InterPro
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells missing tonB survive hydroxyurea treatment better than wild-type; further disruption of mazE-mazF and relE-relB yields even better survival (PubMed:20005847).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Protein TonBPRO_0000196194Add
BLAST

Proteomic databases

PaxDbiP02929.
PRIDEiP02929.

Expressioni

Inductioni

2-fold by hydroxyurea treatment.1 Publication

Interactioni

Subunit structurei

Homodimer. Forms a complex with the accessory proteins ExbB and ExbD.

Binary interactionsi

WithEntry#Exp.IntActNotes
exbBP0ABU72EBI-6399993,EBI-6399986
exbDP0ABV23EBI-6399993,EBI-6417016
fepAP058252EBI-6399993,EBI-6400027
lppP697762EBI-6399993,EBI-909750

Protein-protein interaction databases

BioGridi4262996. 181 interactions.
DIPiDIP-48111N.
IntActiP02929. 5 interactions.
STRINGi511145.b1252.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi155 – 1573Combined sources
Helixi165 – 1706Combined sources
Beta strandi174 – 1829Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi188 – 20215Combined sources
Helixi203 – 2108Combined sources
Beta strandi221 – 23818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHRX-ray1.55A/B164-239[»]
1QXXX-ray2.70A164-239[»]
1U07X-ray1.13A/B150-239[»]
1XX3NMR-A103-239[»]
2GRXX-ray3.30C/D31-239[»]
2GSKX-ray2.10B153-233[»]
DisProtiDP00043.
ProteinModelPortaliP02929.
SMRiP02929. Positions 150-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02929.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati70 – 7121-1
Repeati72 – 7321-2
Repeati74 – 7521-3
Repeati76 – 7721-4
Repeati78 – 7921-5; approximate
Repeati80 – 8121-6
Repeati91 – 9222-1
Repeati93 – 9422-2
Repeati95 – 9622-3
Repeati97 – 9822-4
Repeati99 – 10022-5
Repeati101 – 10222-6

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 81126 X 2 AA approximate tandem repeats of E-PAdd
BLAST
Regioni91 – 102126 X 2 AA tandem repeats of K-PAdd
BLAST

Sequence similaritiesi

Belongs to the TonB family.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410822N. Bacteria.
COG0810. LUCA.
InParanoidiP02929.
KOiK03832.
OMAiFSTETIM.
OrthoDBiEOG64XXKH.

Family and domain databases

InterProiIPR003538. TonB.
IPR006260. TonB_C.
[Graphical view]
PfamiPF03544. TonB_C. 1 hit.
[Graphical view]
PRINTSiPR01374. TONBPROTEIN.
TIGRFAMsiTIGR01352. tonB_Cterm. 1 hit.

Sequencei

Sequence statusi: Complete.

P02929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLDLPRRFP WPTLLSVCIH GAVVAGLLYT SVHQVIELPA PAQPISVTMV
60 70 80 90 100
TPADLEPPQA VQPPPEPVVE PEPEPEPIPE PPKEAPVVIE KPKPKPKPKP
110 120 130 140 150
KPVKKVQEQP KRDVKPVESR PASPFENTAP ARLTSSTATA ATSKPVTSVA
160 170 180 190 200
SGPRALSRNQ PQYPARAQAL RIEGQVKVKF DVTPDGRVDN VQILSAKPAN
210 220 230
MFEREVKNAM RRWRYEPGKP GSGIVVNILF KINGTTEIQ
Length:239
Mass (Da):26,094
Last modified:July 1, 1993 - v2
Checksum:i3B59F39D791AE815
GO

Sequence cautioni

The sequence AAB59066.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60069.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60085.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60093.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60101.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60109.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60117.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60125.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60133.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60141.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60149.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB60157.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511T → A in strain: ECOR 28, ECOR 31, ECOR 37, ECOR 46, ECOR 50, ECOR 52, ECOR 60 and ECOR 71.
Natural varianti70 – 701E → K in strain: ECOR 31.
Natural varianti87 – 871V → A in strain: ECOR 37 and ECOR 71.
Natural varianti102 – 1021P → PKP in strain: ECOR 50.
Natural varianti107 – 1071Missing in strain: ECOR 52 and ECOR 60.
Natural varianti114 – 1141V → I in strain: ECOR 28.
Natural varianti133 – 1331L → P in strain: ECOR 16, ECOR 31, ECOR 46, ECOR 50, ECOR 52 and ECOR 60.
Natural varianti176 – 1761V → I in strain: ECOR 60.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00431 Genomic DNA. Translation: AAB59066.1. Different initiation.
U24195 Genomic DNA. Translation: AAB60069.1. Different initiation.
U24196 Genomic DNA. Translation: AAB60077.1. Different initiation.
U24197 Genomic DNA. Translation: AAB60085.1. Different initiation.
U24198 Genomic DNA. Translation: AAB60093.1. Different initiation.
U24199 Genomic DNA. Translation: AAB60101.1. Different initiation.
U24200 Genomic DNA. Translation: AAB60109.1. Different initiation.
U24201 Genomic DNA. Translation: AAB60117.1. Different initiation.
U24202 Genomic DNA. Translation: AAB60125.1. Different initiation.
U24203 Genomic DNA. Translation: AAB60133.1. Different initiation.
U24204 Genomic DNA. Translation: AAB60141.1. Different initiation.
U24205 Genomic DNA. Translation: AAB60149.1. Different initiation.
U24206 Genomic DNA. Translation: AAB60157.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74334.1.
AP009048 Genomic DNA. Translation: BAA14784.2.
PIRiG64872. BVEC.
RefSeqiNP_415768.1. NC_000913.3.
WP_001360141.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74334; AAC74334; b1252.
BAA14784; BAA14784; BAA14784.
GeneIDi945843.
KEGGiecj:JW5195.
eco:b1252.
PATRICi32117764. VBIEscCol129921_1302.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00431 Genomic DNA. Translation: AAB59066.1. Different initiation.
U24195 Genomic DNA. Translation: AAB60069.1. Different initiation.
U24196 Genomic DNA. Translation: AAB60077.1. Different initiation.
U24197 Genomic DNA. Translation: AAB60085.1. Different initiation.
U24198 Genomic DNA. Translation: AAB60093.1. Different initiation.
U24199 Genomic DNA. Translation: AAB60101.1. Different initiation.
U24200 Genomic DNA. Translation: AAB60109.1. Different initiation.
U24201 Genomic DNA. Translation: AAB60117.1. Different initiation.
U24202 Genomic DNA. Translation: AAB60125.1. Different initiation.
U24203 Genomic DNA. Translation: AAB60133.1. Different initiation.
U24204 Genomic DNA. Translation: AAB60141.1. Different initiation.
U24205 Genomic DNA. Translation: AAB60149.1. Different initiation.
U24206 Genomic DNA. Translation: AAB60157.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74334.1.
AP009048 Genomic DNA. Translation: BAA14784.2.
PIRiG64872. BVEC.
RefSeqiNP_415768.1. NC_000913.3.
WP_001360141.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHRX-ray1.55A/B164-239[»]
1QXXX-ray2.70A164-239[»]
1U07X-ray1.13A/B150-239[»]
1XX3NMR-A103-239[»]
2GRXX-ray3.30C/D31-239[»]
2GSKX-ray2.10B153-233[»]
DisProtiDP00043.
ProteinModelPortaliP02929.
SMRiP02929. Positions 150-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262996. 181 interactions.
DIPiDIP-48111N.
IntActiP02929. 5 interactions.
STRINGi511145.b1252.

Protein family/group databases

TCDBi2.C.1.1.1. the tonb-exbb-exbd/tola-tolq-tolr (tonb) family of auxiliary proteins for energization of outer membrane receptor (omr)-mediated active transport.

Proteomic databases

PaxDbiP02929.
PRIDEiP02929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74334; AAC74334; b1252.
BAA14784; BAA14784; BAA14784.
GeneIDi945843.
KEGGiecj:JW5195.
eco:b1252.
PATRICi32117764. VBIEscCol129921_1302.

Organism-specific databases

EchoBASEiEB1005.
EcoGeneiEG11012. tonB.

Phylogenomic databases

eggNOGiENOG410822N. Bacteria.
COG0810. LUCA.
InParanoidiP02929.
KOiK03832.
OMAiFSTETIM.
OrthoDBiEOG64XXKH.

Enzyme and pathway databases

BioCyciEcoCyc:EG11012-MONOMER.
ECOL316407:JW5195-MONOMER.
MetaCyc:EG11012-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02929.
PROiP02929.

Family and domain databases

InterProiIPR003538. TonB.
IPR006260. TonB_C.
[Graphical view]
PfamiPF03544. TonB_C. 1 hit.
[Graphical view]
PRINTSiPR01374. TONBPROTEIN.
TIGRFAMsiTIGR01352. tonB_Cterm. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of the Escherichia coli tonB gene."
    Postle K., Good R.F.
    Proc. Natl. Acad. Sci. U.S.A. 80:5235-5239(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Milkman R.
    Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 and Various ECOR strains.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions."
    Roof S.K., Allard J.D., Bertrand K.P., Postel K.
    J. Bacteriol. 173:5554-5557(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  7. "A sequence-specific function for the N-terminal signal-like sequence of the TonB protein."
    Karlsson M., Hannavy K., Higgins C.F.
    Mol. Microbiol. 8:379-388(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPORTANCE OF N-TERMINAL SEQUENCE.
  8. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY HYDROXYUREA, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  9. "Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold."
    Chang C., Mooser A., Plueckthun A., Wlodawer A.
    J. Biol. Chem. 276:27535-27540(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 164-239.

Entry informationi

Entry nameiTONB_ECOLI
AccessioniPrimary (citable) accession number: P02929
Secondary accession number(s): P76831
, P94719, P94722, P94726, P94728, P94732, P94736, P94739, P97239
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.