TONB_ECOLI
ID TONB_ECOLI Reviewed; 239 AA.
AC P02929; P76831; P94719; P94722; P94726; P94728; P94732; P94736; P94739;
AC P97239;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein TonB;
GN Name=tonB; Synonyms=exbA; OrderedLocusNames=b1252, JW5195;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6310567; DOI=10.1073/pnas.80.17.5235;
RA Postle K., Good R.F.;
RT "DNA sequence of the Escherichia coli tonB gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:5235-5239(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12, and Various ECOR strains;
RA Milkman R.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP TOPOLOGY.
RX PubMed=1885532; DOI=10.1128/jb.173.17.5554-5557.1991;
RA Roof S.K., Allard J.D., Bertrand K.P., Postel K.;
RT "Analysis of Escherichia coli TonB membrane topology by use of PhoA
RT fusions.";
RL J. Bacteriol. 173:5554-5557(1991).
RN [7]
RP IMPORTANCE OF N-TERMINAL SEQUENCE.
RX PubMed=8316087; DOI=10.1111/j.1365-2958.1993.tb01581.x;
RA Karlsson M., Hannavy K., Higgins C.F.;
RT "A sequence-specific function for the N-terminal signal-like sequence of
RT the TonB protein.";
RL Mol. Microbiol. 8:379-388(1993).
RN [8]
RP FUNCTION, INDUCTION BY HYDROXYUREA, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 164-239.
RX PubMed=11328822; DOI=10.1074/jbc.m102778200;
RA Chang C., Mooser A., Plueckthun A., Wlodawer A.;
RT "Crystal structure of the dimeric C-terminal domain of TonB reveals a novel
RT fold.";
RL J. Biol. Chem. 276:27535-27540(2001).
CC -!- FUNCTION: Interacts with outer membrane receptor proteins that carry
CC out high-affinity binding and energy dependent uptake into the
CC periplasmic space of specific substrates such as cobalamin, and various
CC iron compounds (such as iron dicitrate, enterochelin, aerobactin,
CC etc.). In the absence of TonB these receptors bind their substrates but
CC do not carry out active transport. TonB also interacts with some
CC colicins and is involved in the energy-dependent, irreversible steps of
CC bacteriophages phi 80 and T1 infection. It could act to transduce
CC energy from the cytoplasmic membrane to specific energy-requiring
CC processes in the outer membrane, resulting in the release into the
CC periplasm of ligands bound by these outer membrane proteins. Implicated
CC in hydroxy radical-mediated cell death induced by hydroxyurea treatment
CC (PubMed:20005847). {ECO:0000269|PubMed:20005847}.
CC -!- SUBUNIT: Homodimer. Forms a complex with the accessory proteins ExbB
CC and ExbD.
CC -!- INTERACTION:
CC P02929; P0ABU7: exbB; NbExp=2; IntAct=EBI-6399993, EBI-6399986;
CC P02929; P0ABV2: exbD; NbExp=3; IntAct=EBI-6399993, EBI-6417016;
CC P02929; P13036: fecA; NbExp=3; IntAct=EBI-6399993, EBI-1131517;
CC P02929; P05825: fepA; NbExp=2; IntAct=EBI-6399993, EBI-6400027;
CC P02929; P06971: fhuA; NbExp=4; IntAct=EBI-6399993, EBI-1116714;
CC P02929; P69776: lpp; NbExp=2; IntAct=EBI-6399993, EBI-909750;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC protein; Periplasmic side.
CC -!- INDUCTION: 2-fold by hydroxyurea treatment.
CC {ECO:0000269|PubMed:20005847}.
CC -!- DISRUPTION PHENOTYPE: Cells missing tonB survive hydroxyurea treatment
CC better than wild-type; further disruption of mazE-mazF and relE-relB
CC yields even better survival (PubMed:20005847).
CC {ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the TonB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59066.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60069.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60077.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60085.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60093.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60101.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60109.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60117.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60125.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60133.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60141.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60149.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB60157.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; K00431; AAB59066.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24195; AAB60069.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24196; AAB60077.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24197; AAB60085.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24198; AAB60093.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24199; AAB60101.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24200; AAB60109.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24201; AAB60117.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24202; AAB60125.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24203; AAB60133.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24204; AAB60141.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24205; AAB60149.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24206; AAB60157.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74334.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14784.2; -; Genomic_DNA.
DR PIR; G64872; BVEC.
DR RefSeq; NP_415768.1; NC_000913.3.
DR RefSeq; WP_001360141.1; NZ_SSZK01000031.1.
DR PDB; 1IHR; X-ray; 1.55 A; A/B=164-239.
DR PDB; 1QXX; X-ray; 2.70 A; A=164-239.
DR PDB; 1U07; X-ray; 1.13 A; A/B=150-239.
DR PDB; 1XX3; NMR; -; A=103-239.
DR PDB; 2GRX; X-ray; 3.30 A; C/D=31-239.
DR PDB; 2GSK; X-ray; 2.10 A; B=153-233.
DR PDBsum; 1IHR; -.
DR PDBsum; 1QXX; -.
DR PDBsum; 1U07; -.
DR PDBsum; 1XX3; -.
DR PDBsum; 2GRX; -.
DR PDBsum; 2GSK; -.
DR AlphaFoldDB; P02929; -.
DR BMRB; P02929; -.
DR SMR; P02929; -.
DR BioGRID; 4262996; 186.
DR BioGRID; 850210; 1.
DR ComplexPortal; CPX-1083; Cobalamin outer membrane transporter complex.
DR ComplexPortal; CPX-2843; Ferrichrome outer membrane transporter complex.
DR ComplexPortal; CPX-3576; Ferric-citrate outer membrane transporter complex.
DR ComplexPortal; CPX-3577; Ferric-catecholate outer membrane transporter complex.
DR ComplexPortal; CPX-3578; Ferric-enterobactin outer membrane transporter complex.
DR ComplexPortal; CPX-3579; Ferric-coprogen outer membrane transporter complex.
DR ComplexPortal; CPX-3580; fiu outer membrane transporter complex.
DR ComplexPortal; CPX-3585; Uncharacterized yncD-DHBS outer membrane transporter complex.
DR DIP; DIP-48111N; -.
DR IntAct; P02929; 8.
DR STRING; 511145.b1252; -.
DR DrugBank; DB02767; (R)-3-hydroxytetradecanoic acid.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB08231; Myristic acid.
DR TCDB; 2.C.1.1.1; the tonb-exbb-exbd/tola-tolq-tolr outer membrane receptor energizers and stabilizers (tonb/tola) family.
DR jPOST; P02929; -.
DR PaxDb; P02929; -.
DR PRIDE; P02929; -.
DR EnsemblBacteria; AAC74334; AAC74334; b1252.
DR EnsemblBacteria; BAA14784; BAA14784; BAA14784.
DR GeneID; 945843; -.
DR KEGG; ecj:JW5195; -.
DR KEGG; eco:b1252; -.
DR PATRIC; fig|511145.12.peg.1302; -.
DR EchoBASE; EB1005; -.
DR eggNOG; COG0810; Bacteria.
DR HOGENOM; CLU_098618_0_0_6; -.
DR InParanoid; P02929; -.
DR OMA; DCYLHLK; -.
DR PhylomeDB; P02929; -.
DR BioCyc; EcoCyc:EG11012-MON; -.
DR BioCyc; MetaCyc:EG11012-MON; -.
DR EvolutionaryTrace; P02929; -.
DR PRO; PR:P02929; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030313; C:cell envelope; IDA:CACAO.
DR GO; GO:0009279; C:cell outer membrane; IC:ComplexPortal.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0031992; F:energy transducer activity; IDA:EcoCyc.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0015343; F:siderophore transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015889; P:cobalamin transport; IMP:EcoCyc.
DR GO; GO:0042914; P:colicin transport; TAS:EcoCyc.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0055065; P:metal ion homeostasis; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0098002; P:receptor-mediated bacteriophage irreversible attachment to host cell; TAS:EcoCyc.
DR GO; GO:0015891; P:siderophore transport; IDA:EcoCyc.
DR DisProt; DP00043; -.
DR InterPro; IPR003538; TonB.
DR InterPro; IPR006260; TonB/TolA_C.
DR InterPro; IPR037682; TonB_C.
DR Pfam; PF03544; TonB_C; 1.
DR PRINTS; PR01374; TONBPROTEIN.
DR TIGRFAMs; TIGR01352; tonB_Cterm; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacteriocin transport; Cell inner membrane; Cell membrane;
KW Membrane; Protein transport; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..239
FT /note="Protein TonB"
FT /id="PRO_0000196194"
FT TRANSMEM 1..32
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000305"
FT TOPO_DOM 33..239
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1885532"
FT REPEAT 70..71
FT /note="1-1"
FT REPEAT 72..73
FT /note="1-2"
FT REPEAT 74..75
FT /note="1-3"
FT REPEAT 76..77
FT /note="1-4"
FT REPEAT 78..79
FT /note="1-5; approximate"
FT REPEAT 80..81
FT /note="1-6"
FT REPEAT 91..92
FT /note="2-1"
FT REPEAT 93..94
FT /note="2-2"
FT REPEAT 95..96
FT /note="2-3"
FT REPEAT 97..98
FT /note="2-4"
FT REPEAT 99..100
FT /note="2-5"
FT REPEAT 101..102
FT /note="2-6"
FT REGION 55..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..81
FT /note="6 X 2 AA approximate tandem repeats of E-P"
FT REGION 91..102
FT /note="6 X 2 AA tandem repeats of K-P"
FT COMPBIAS 57..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 51
FT /note="T -> A (in strain: ECOR 28, ECOR 31, ECOR 37, ECOR
FT 46, ECOR 50, ECOR 52, ECOR 60 and ECOR 71)"
FT VARIANT 70
FT /note="E -> K (in strain: ECOR 31)"
FT VARIANT 87
FT /note="V -> A (in strain: ECOR 37 and ECOR 71)"
FT VARIANT 102
FT /note="P -> PKP (in strain: ECOR 50)"
FT VARIANT 107
FT /note="Missing (in strain: ECOR 52 and ECOR 60)"
FT VARIANT 114
FT /note="V -> I (in strain: ECOR 28)"
FT VARIANT 133
FT /note="L -> P (in strain: ECOR 16, ECOR 31, ECOR 46, ECOR
FT 50, ECOR 52 and ECOR 60)"
FT VARIANT 176
FT /note="V -> I (in strain: ECOR 60)"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1U07"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:1U07"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:1U07"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1QXX"
FT STRAND 188..202
FT /evidence="ECO:0007829|PDB:1U07"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:1U07"
FT STRAND 221..238
FT /evidence="ECO:0007829|PDB:1U07"
SQ SEQUENCE 239 AA; 26094 MW; 3B59F39D791AE815 CRC64;
MTLDLPRRFP WPTLLSVCIH GAVVAGLLYT SVHQVIELPA PAQPISVTMV TPADLEPPQA
VQPPPEPVVE PEPEPEPIPE PPKEAPVVIE KPKPKPKPKP KPVKKVQEQP KRDVKPVESR
PASPFENTAP ARLTSSTATA ATSKPVTSVA SGPRALSRNQ PQYPARAQAL RIEGQVKVKF
DVTPDGRVDN VQILSAKPAN MFEREVKNAM RRWRYEPGKP GSGIVVNILF KINGTTEIQ
