ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P02930


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TOLC_ECOLI
Primary accession number P02930
Secondary accession number Q2M9G5
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on June 27, 2006 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 101)
Name and origin of the protein
Protein name Outer membrane protein tolC [Precursor]
Synonyms None
Gene name
Name: tolC
Synonyms: mtcB, mukA, refI
OrderedLocusNames: b3035, JW5503
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/11.18.6487; PubMed=6312426 [NCBI, ExPASy, EBI, Israel, Japan]
Hackett J., Reeves P.;
"Primary structure of the tolC gene that codes for an outer membrane protein of Escherichia coli K12.";
Nucleic Acids Res. 11:6487-6495(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/18.18.5547; PubMed=2216730 [NCBI, ExPASy, EBI, Israel, Japan]
Niki H., Imamura R., Ogura T., Hiraga S.;
"Nucleotide sequence of the tolC gene of Escherichia coli.";
Nucleic Acids Res. 18:5547-5547(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
STRAIN=K12;
DOI=10.1016/0014-5793(83)80518-3; PubMed=6303857 [NCBI, ExPASy, EBI, Israel, Japan]
Hackett J., Misra R., Reeves P.;
"The TolC protein of Escherichia coli K12 is synthesised in a precursor form.";
FEBS Lett. 156:307-310(1983).
[6]
PROTEIN SEQUENCE OF 23-34.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
PROTEIN SEQUENCE OF 23-27.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1002/elps.1150190539; PubMed=9629924 [NCBI, ExPASy, EBI, Israel, Japan]
Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
"Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis.";
Electrophoresis 19:837-844(1998).
[8]
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
DOI=10.1074/jbc.M506479200; PubMed=16079137 [NCBI, ExPASy, EBI, Israel, Japan]
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-450.
DOI=10.1038/35016007; PubMed=10879525 [NCBI, ExPASy, EBI, Israel, Japan]
Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C.;
"Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export.";
Nature 405:914-919(2000).
Comments
  • FUNCTION: Required for proper expression of outer membrane protein genes such as ompF, nmpC, protein 2, hemolysin, colicin V, or colicin E1. May be specialized for signal sequence independent, extracellular secretion in Gram-negative bacteria.
  • SUBUNIT: Homotrimer that assembles to form a continuous, solvent-accessible conduit: a 'channel-tunnel' over 140 Angstroms long that spans both the outer membrane and periplasmic space. The periplasmic or proximal end of the tunnel is sealed by sets of coiled helices.
  • SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
  • SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family [view classification].
  • SEQUENCE CAUTION:
    • Sequence=CAA24914.1; Type=Miscellaneous discrepancy;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X00016; CAA24914.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54049; CAA37982.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28377; AAA69203.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76071.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77091.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01505; CAA24751.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A65091; MMECTC.
RefSeq AP_003585.1; -.
NP_417507.2; -.
3D structure databases
PDB
1EK9; X-ray; 2.10 A; A/B/C=23-450.[ExPASy / RCSB / EBI]
1TQQ; X-ray; 2.75 A; A/B/C=23-493.[ExPASy / RCSB / EBI]
1TTQ; X-ray; 2.00 A; A=-, B=1-12.[ExPASy / RCSB / EBI]
2VDD; X-ray; 3.30 A; A/B/C=3-450.[ExPASy / RCSB / EBI]
2VDE; X-ray; 3.20 A; A/B/C=3-450.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EK9; -.
1TQQ; -.
1TTQ; -.
2VDD; -.
2VDE; -.
ModBase P02930.
Protein-protein interaction databases
DIP DIP:11007N; -.
IntAct P02930; 2.
Protein family/group databases
TCDB 1.B.17.1.1; outer membrane factor (OMF) family.
Enzyme and pathway databases
BioCyc EcoCyc:EG11009-MON; -.
2D gel databases
SWISS-2DPAGE P02930; -.
2DBase-Ecoli P02930; -.
Organism-specific databases
EchoBASE EB1002; -.
EcoGene EG11009; tolC.
Ontologies
GO
GO:0009279; Cellular component: cell outer membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005215; Molecular function: transporter activity (inferred from electronic annotation from InterPro).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003423; OMP_efflux.
IPR010130; T1SS_OMP_TolC.
Graphical view of domain structure.
Pfam PF02321; OEP; 2.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01844; type_I_sec_TolC; 1.
Genome annotation databases
GeneID 947521; -.
GenomeReviews AP009048_GR; JW5503.
U00096_GR; b3035.
KEGG ecj:JW5503; -.
eco:b3035; -.
Phylogenomic databases
HOGENOM P02930; -.
OMA P02930; AMSQAEN.
Genome annotation databases
CMR P02930; b3035.
Other
ProtoNet P02930.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Cell outer membrane; Complete proteome; Direct protein sequencing; Membrane; Repeat; Signal; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
CHAIN   23   493  471     Outer membrane protein tolC. PRO_0000013352
TOPO_DOM   23    62  40     Periplasmic. 
TRANSMEM   63    74  12     S1. 
TOPO_DOM   75    82  8     Extracellular. 
TRANSMEM   83    96  14     S2. 
TOPO_DOM   97   268  172     Periplasmic. 
TRANSMEM   269   279  11     S4. 
TOPO_DOM   280   300  21     Extracellular. 
TRANSMEM   301   311  11     S5. 
TOPO_DOM   312   493  182     Periplasmic. 
REPEAT   23   230  208     1. 
REPEAT   231   446  216     2. 
CONFLICT   191   191        V -> L (in Ref. 1; CAA37982). 
HELIX   25    35  11      
HELIX   37    57  21      
HELIX   58    60  3      
STRAND   63    75  13      
STRAND   77    79  3      
STRAND   83    98  16      
HELIX   100   167  68      
HELIX   173   208  36      
STRAND   213   218  6      
TURN   220   222  3      
HELIX   231   241  11      
HELIX   243   263  21      
HELIX   264   266  3      
STRAND   269   279  11      
STRAND   282   285  4      
STRAND   288   291  4      
STRAND   302   316  15      
HELIX   319   385  67      
HELIX   391   426  36      
HELIX   431   439  9      
STRAND   441   448  8      
Sequence information
Length: 493 AA [This is the length of the unprocessed precursor] Molecular weight: 53741 Da [This is the MW of the unprocessed precursor] CRC64: 6F97B4C62A848FE1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKLLPILIG LSLSGFSSLS QAENLMQVYQ QARLSNPELR KSAADRDAAF EKINEARSPL 

        70         80         90        100        110        120 
LPQLGLGADY TYSNGYRDAN GINSNATSAS LQLTQSIFDM SKWRALTLQE KAAGIQDVTY 

       130        140        150        160        170        180 
QTDQQTLILN TATAYFNVLN AIDVLSYTQA QKEAIYRQLD QTTQRFNVGL VAITDVQNAR 

       190        200        210        220        230        240 
AQYDTVLANE VTARNNLDNA VEQLRQITGN YYPELAALNV ENFKTDKPQP VNALLKEAEK 

       250        260        270        280        290        300 
RNLSLLQARL SQDLAREQIR QAQDGHLPTL DLTASTGISD TSYSGSKTRG AAGTQYDDSN 

       310        320        330        340        350        360 
MGQNKVGLSF SLPIYQGGMV NSQVKQAQYN FVGASEQLES AHRSVVQTVR SSFNNINASI 

       370        380        390        400        410        420 
SSINAYKQAV VSAQSSLDAM EAGYSVGTRT IVDVLDATTT LYNAKQELAN ARYNYLINQL 

       430        440        450        460        470        480 
NIKSALGTLN EQDLLALNNA LSKPVSTNPE NVAPQTPEQN AIADGYAPDS PAPVVQQTSA 

       490 
RTTTSNGHNP FRN 

P02930 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!