UniProtKB - P02930 (TOLC_ECOLI)

BLAST

>sp|P02930|TOLC_ECOLI Outer membrane protein TolC OS=Escherichia coli (strain K12) OX=83333 GN=tolC PE=1 SV=3
MKKLLPILIGLSLSGFSSLSQAENLMQVYQQARLSNPELRKSAADRDAAFEKINEARSPL
LPQLGLGADYTYSNGYRDANGINSNATSASLQLTQSIFDMSKWRALTLQEKAAGIQDVTY
QTDQQTLILNTATAYFNVLNAIDVLSYTQAQKEAIYRQLDQTTQRFNVGLVAITDVQNAR
AQYDTVLANEVTARNNLDNAVEQLRQITGNYYPELAALNVENFKTDKPQPVNALLKEAEK
RNLSLLQARLSQDLAREQIRQAQDGHLPTLDLTASTGISDTSYSGSKTRGAAGTQYDDSN
MGQNKVGLSFSLPIYQGGMVNSQVKQAQYNFVGASEQLESAHRSVVQTVRSSFNNINASI
SSINAYKQAVVSAQSSLDAMEAGYSVGTRTIVDVLDATTTLYNAKQELANARYNYLINQL
NIKSALGTLNEQDLLALNNALSKPVSTNPENVAPQTPEQNAIADGYAPDSPAPVVQQTSA
RTTTSNGHNPFRN

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History
Entry version 176 (12 Sep 2018)
Sequence version 3 (27 Jun 2006)
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Protein

Outer membrane protein TolC

Gene

tolC

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.5 Publications

Activity regulationⁱ

In vitro, inhibited by hexaamminecobalt³⁺.1 Publication

GO - Molecular functionⁱ

efflux transmembrane transporter activity
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 2112747
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
ion channel activity
Source: CAFA
Inferred from direct assayⁱ
- 15465872
porin activity
Source: EcoCyc
Inferred from direct assayⁱ
- 7688606
protein N-terminus binding
Source: CAFA
Inferred from physical interactionⁱ
- 15465872

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

drug export
Source: EcoCyc
Inferred from direct assayⁱ
- 28504659
enterobactin transport
Source: EcoliWiki
Inferred from genetic interactionⁱ
- 16166532
ion transmembrane transport
Source: CAFA
Inferred from direct assayⁱ
- 15465872
response to antibiotic Source: UniProtKB-KW
response to organic cyclic compound
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 9473050

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Antibiotic resistance, Transport

Biological process

Antibiotic resistance, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11009-MONOMER MetaCyc:EG11009-MONOMER

BioCycⁱ

EcoCyc:EG11009-MONOMER
MetaCyc:EG11009-MONOMER

Protein family/group databases

TCDBⁱ	1.B.17.1.1 the outer membrane factor (omf) family

TCDBⁱ

1.B.17.1.1 the outer membrane factor (omf) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Outer membrane protein TolC Alternative name(s): Multidrug efflux pump subunit TolC Outer membrane factor TolC
Gene namesⁱ	Name:tolC Synonyms:colE1-i, mtcB, mukA, refI, toc, weeA Ordered Locus Names:b3035, JW5503
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11009 tolC

EcoGeneⁱ

EG11009 tolC

Subcellular locationⁱ

Cell outer membrane
5 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "Identification and characterization of the TolC protein, an outer membrane protein from Escherichia coli."
  Morona R., Manning P.A., Reeves P.
  J. Bacteriol. 153:693-699(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 23-34, FUNCTION, SUBCELLULAR LOCATION.
- Ref.9
  "Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals."
  Koronakis V., Li J., Koronakis E., Stauffer K.
  Mol. Microbiol. 23:617-626(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
- Ref.11
  "Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system."
  Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.
  Mol. Microbiol. 53:697-706(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN ACRAB-TOLC EFFLUX SYSTEM, INTERACTION WITH ACRA, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
- Ref.12
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
- Ref.17
  "Membrane localization of small proteins in Escherichia coli."
  Fontaine F., Fuchs R.T., Storz G.
  J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
; Multi-pass membrane protein
5 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "Identification and characterization of the TolC protein, an outer membrane protein from Escherichia coli."
  Morona R., Manning P.A., Reeves P.
  J. Bacteriol. 153:693-699(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 23-34, FUNCTION, SUBCELLULAR LOCATION.
- Ref.9
  "Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals."
  Koronakis V., Li J., Koronakis E., Stauffer K.
  Mol. Microbiol. 23:617-626(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
- Ref.11
  "Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system."
  Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.
  Mol. Microbiol. 53:697-706(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN ACRAB-TOLC EFFLUX SYSTEM, INTERACTION WITH ACRA, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
- Ref.12
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
- Ref.17
  "Membrane localization of small proteins in Escherichia coli."
  Fontaine F., Fuchs R.T., Storz G.
  J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	23 – 62	PeriplasmicAdd BLAST	40
Transmembraneⁱ	63 – 74	Beta stranded; Name=S1Add BLAST	12
Topological domainⁱ	75 – 82	Extracellular	8
Transmembraneⁱ	83 – 96	Beta stranded; Name=S2Add BLAST	14
Topological domainⁱ	97 – 268	PeriplasmicAdd BLAST	172
Transmembraneⁱ	269 – 279	Beta stranded; Name=S4Add BLAST	11
Topological domainⁱ	280 – 300	ExtracellularAdd BLAST	21
Transmembraneⁱ	301 – 311	Beta stranded; Name=S5Add BLAST	11
Topological domainⁱ	312 – 493	PeriplasmicAdd BLAST	182

GO - Cellular componentⁱ

cell outer membrane
Source: EcoCyc
Inferred from direct assayⁱ
efflux pump complex
Source: EcoCyc
Inferred from physical interactionⁱ
- 15155734
integral component of membrane
Source: CAFA
Inferred from direct assayⁱ
- 15465872
MacAB-TolC complex
Source: EcoCyc
Inferred from direct assayⁱ
- 28504659

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell outer membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Cannot grow on efflux substrates novobiocin or fusidic acid.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	384	Y → F: Partial channel opening. Increases sensitivity to vancomycin, by allowing its passive diffusion across the outer membrane; when associated with E-389. 1 Publication	1
Mutagenesisⁱ	389	R → E: Partial channel opening. Increases sensitivity to vancomycin, by allowing its passive diffusion across the outer membrane; when associated with F-382. 1 Publication	1
Mutagenesisⁱ	393	D → A: Decreases inhibition by hexaamminecobalt(3+). 1 Publication	1
Mutagenesisⁱ	396	D → A: Decreases inhibition by hexaamminecobalt(3+). 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL3309023
Drug and drug target database More...DrugBankⁱ	DB03350 Cobalt Hexammine Ion

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 22	3 PublicationsAdd BLAST		22
ChainⁱPRO_0000013352	23 – 493	Outer membrane protein TolCAdd BLAST		471

Proteomic databases

EPDⁱ	P02930
PaxDbⁱ	P02930
PRIDEⁱ	P02930

2D gel databases

SWISS-2DPAGEⁱ	P02930

SWISS-2DPAGEⁱ

P02930

Interactionⁱ

Subunit structureⁱ

Homotrimer. Part of tripartite efflux systems, which are composed of an inner membrane transporter, a periplasmic membrane fusion protein, and an outer membrane component, TolC. The complexes form a large protein conduit and can translocate molecules across both the inner and outer membranes. TolC interacts with the membrane fusion proteins AcrA, EmrA and MacA.8 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		6	EBI-875614,EBI-875614
acrA	P0AE06	2	EBI-875614,EBI-875601
macA	P75830	2	EBI-875614,EBI-551961

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4263248, 406 interactors
ComplexPortalⁱ	CPX-2107 MacAB-TolC complex
Database of interacting proteins More...DIPⁱ	DIP-11007N
IntActⁱ	P02930, 6 interactors
Molecular INTeraction database More...MINTⁱ	P02930
STRINGⁱ	316385.ECDH10B_3209

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	25 – 35	Combined sources	11
Helixⁱ	37 – 57	Combined sources	21
Helixⁱ	58 – 60	Combined sources	3
Beta strandⁱ	63 – 75	Combined sources	13
Beta strandⁱ	77 – 79	Combined sources	3
Beta strandⁱ	83 – 98	Combined sources	16
Helixⁱ	100 – 167	Combined sources	68
Beta strandⁱ	168 – 170	Combined sources	3
Helixⁱ	173 – 208	Combined sources	36
Beta strandⁱ	213 – 218	Combined sources	6
Turnⁱ	220 – 222	Combined sources	3
Helixⁱ	231 – 241	Combined sources	11
Helixⁱ	243 – 263	Combined sources	21
Helixⁱ	264 – 266	Combined sources	3
Beta strandⁱ	269 – 279	Combined sources	11
Beta strandⁱ	282 – 285	Combined sources	4
Beta strandⁱ	288 – 291	Combined sources	4
Beta strandⁱ	293 – 297	Combined sources	5
Beta strandⁱ	302 – 316	Combined sources	15
Helixⁱ	319 – 385	Combined sources	67
Beta strandⁱ	386 – 388	Combined sources	3
Helixⁱ	391 – 426	Combined sources	36
Helixⁱ	431 – 439	Combined sources	9
Beta strandⁱ	441 – 448	Combined sources	8

Show more details

3D structure databases

ProteinModelPortalⁱ	P02930
SMRⁱ	P02930
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P02930

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Repeatⁱ	23 – 230	1Add BLAST		208
Repeatⁱ	231 – 446	2Add BLAST		216

Domainⁱ

Forms 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.1 Publication

Sequence similaritiesⁱ

Belongs to the outer membrane factor (OMF) (TC 1.B.17) family. [View classification]Curated

Keywords - Domainⁱ

Repeat, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGⁱ	ENOG4105DFG Bacteria COG1538 LUCA
HOGENOMⁱ	HOG000283506
InParanoidⁱ	P02930
KEGG Orthology (KO) More...KOⁱ	K12340
OMAⁱ	YNAKQQL
PhylomeDBⁱ	P02930

Family and domain databases

InterProⁱ	View protein in InterPro IPR003423 OMP_efflux IPR010130 T1SS_OMP_TolC
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02321 OEP, 2 hits
TIGRFAMsⁱ	TIGR01844 type_I_sec_TolC, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P02930-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKKLLPILIG LSLSGFSSLS QAENLMQVYQ QARLSNPELR KSAADRDAAF 
        60         70         80         90        100
EKINEARSPL LPQLGLGADY TYSNGYRDAN GINSNATSAS LQLTQSIFDM 
       110        120        130        140        150
SKWRALTLQE KAAGIQDVTY QTDQQTLILN TATAYFNVLN AIDVLSYTQA 
       160        170        180        190        200
QKEAIYRQLD QTTQRFNVGL VAITDVQNAR AQYDTVLANE VTARNNLDNA 
       210        220        230        240        250
VEQLRQITGN YYPELAALNV ENFKTDKPQP VNALLKEAEK RNLSLLQARL 
       260        270        280        290        300
SQDLAREQIR QAQDGHLPTL DLTASTGISD TSYSGSKTRG AAGTQYDDSN 
       310        320        330        340        350
MGQNKVGLSF SLPIYQGGMV NSQVKQAQYN FVGASEQLES AHRSVVQTVR 
       360        370        380        390        400
SSFNNINASI SSINAYKQAV VSAQSSLDAM EAGYSVGTRT IVDVLDATTT 
       410        420        430        440        450
LYNAKQELAN ARYNYLINQL NIKSALGTLN EQDLLALNNA LSKPVSTNPE 
       460        470        480        490 
NVAPQTPEQN AIADGYAPDS PAPVVQQTSA RTTTSNGHNP FRN

Length:493

Mass (Da):53,741

Last modified:June 27, 2006 - v3

Checksum:ⁱ6F97B4C62A848FE1

Sequence cautionⁱ

The sequence AAA69203 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

The sequence CAA24751 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

The sequence CAA37982 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	178	N → K in CAA24914 (PubMed:6312426).Curated	1
Sequence conflictⁱ	191	V → L in CAA37982 (PubMed:2216730).Curated	1
Sequence conflictⁱ	203 – 204	QL → HV in CAA24914 (PubMed:6312426).Curated	2
Sequence conflictⁱ	214 – 215	EL → GT in CAA24914 (PubMed:6312426).Curated	2
Sequence conflictⁱ	258 – 270	QIRQA…HLPTL → KFARRRMVTYRLW in CAA24914 (PubMed:6312426).CuratedAdd BLAST	13
Sequence conflictⁱ	278 – 295	ISDTS…AAGTQ → FLTPLIAVRKPCAAVP in CAA24914 (PubMed:6312426).CuratedAdd BLAST	18
Sequence conflictⁱ	325	K → T in CAA24914 (PubMed:6312426).Curated	1
Sequence conflictⁱ	335 – 354	SEQLE…RSSFN → ASTWKVPIVASCQRAFCFS in CAA24914 (PubMed:6312426).CuratedAdd BLAST	20
Sequence conflictⁱ	365 – 370	AYKQAV → RYTQAA in CAA24914 (PubMed:6312426).Curated	6
Sequence conflictⁱ	400 – 411	TLYNA…ELANA → SCTAQARAGNP in CAA24914 (PubMed:6312426).CuratedAdd BLAST	12
Sequence conflictⁱ	445	V → I in CAA24914 (PubMed:6312426).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X00016 Genomic DNA Translation: CAA24914.1 X54049 Genomic DNA Translation: CAA37982.1 Different initiation. U28377 Genomic DNA Translation: AAA69203.1 Different initiation. U00096 Genomic DNA Translation: AAC76071.2 AP009048 Genomic DNA Translation: BAE77091.1 V01505 Genomic DNA Translation: CAA24751.1 Different initiation.
PIRⁱ	A65091 MMECTC
NCBI Reference Sequences More...RefSeqⁱ	NP_417507.2, NC_000913.3 WP_000735278.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76071; AAC76071; b3035 BAE77091; BAE77091; BAE77091
GeneIDⁱ	947521
KEGGⁱ	ecj:JW5503 eco:b3035
PATRICⁱ	fig\|1411691.4.peg.3696

Protein	Similar proteins		Species	Score	Length	Source
P02930	Outer membrane channel TolC		ECOLX		495	UniRef100_P02930
Outer membrane protein TolC		ECOCB		506
Outer membrane channel protein		Escherichia coli D9		506
OEP domain containing protein		TRITR		495
Outer membrane channel protein		Escherichia coli MS 145-7		495
+111

Protein	Similar proteins		Species	Score	Length	Source
P02930	Outer membrane channel TolC		ECOLX		495	UniRef90_P02930
Outer membrane protein TolC		ECOCB		506
Outer membrane channel protein		Escherichia coli D9		506
OEP domain containing protein		TRITR		495
Outer membrane channel protein		Escherichia coli MS 145-7		495
+739

Protein	Similar proteins		Species	Score	Length	Source
P02930	Outer membrane protein TolC		SALEN		491	UniRef50_P02930
Outer membrane channel TolC		ECOLX		495
Outer membrane protein TolC		ECOCB		506
Outer membrane channel protein		Escherichia coli D9		506
OEP domain containing protein		TRITR		495
+1667

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X00016 Genomic DNA Translation: CAA24914.1 X54049 Genomic DNA Translation: CAA37982.1 Different initiation. U28377 Genomic DNA Translation: AAA69203.1 Different initiation. U00096 Genomic DNA Translation: AAC76071.2 AP009048 Genomic DNA Translation: BAE77091.1 V01505 Genomic DNA Translation: CAA24751.1 Different initiation.
PIRⁱ	A65091 MMECTC
RefSeqⁱ	NP_417507.2, NC_000913.3 WP_000735278.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1EK9	X-ray	2.10	A/B/C	23-450	[»]
	1TQQ	X-ray	2.75	A/B/C	23-493	[»]
	2VDD	X-ray	3.30	A/B/C	1-450	[»]
	2VDE	X-ray	3.20	A/B/C	1-450	[»]
	2WMZ	X-ray	2.90	A/B/C	23-450	[»]
	2XMN	X-ray	2.85	A/B/C	23-450	[»]
	5NG5	electron microscopy	6.50	C/F/I	1-493	[»]
	5NIK	electron microscopy	3.30	A/B/C	23-493	[»]
	5NIL	electron microscopy	5.30	A/B/C	23-493	[»]
	5O66	electron microscopy	5.90	A/B/C	1-493	[»]
	5V5S	electron microscopy	6.50	A/B/C	23-464	[»]
ProteinModelPortalⁱ	P02930
SMRⁱ	P02930
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263248, 406 interactors
ComplexPortalⁱ	CPX-2107 MacAB-TolC complex
DIPⁱ	DIP-11007N
IntActⁱ	P02930, 6 interactors
MINTⁱ	P02930
STRINGⁱ	316385.ECDH10B_3209

Chemistry databases

ChEMBLⁱ	CHEMBL3309023
DrugBankⁱ	DB03350 Cobalt Hexammine Ion

Protein family/group databases

TCDBⁱ	1.B.17.1.1 the outer membrane factor (omf) family

TCDBⁱ

1.B.17.1.1 the outer membrane factor (omf) family

2D gel databases

SWISS-2DPAGEⁱ	P02930

SWISS-2DPAGEⁱ

P02930

Proteomic databases

EPDⁱ	P02930
PaxDbⁱ	P02930
PRIDEⁱ	P02930

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76071; AAC76071; b3035 BAE77091; BAE77091; BAE77091
GeneIDⁱ	947521
KEGGⁱ	ecj:JW5503 eco:b3035
PATRICⁱ	fig\|1411691.4.peg.3696

Organism-specific databases

EchoBASEⁱ	EB1002
EcoGeneⁱ	EG11009 tolC

Phylogenomic databases

eggNOGⁱ	ENOG4105DFG Bacteria COG1538 LUCA
HOGENOMⁱ	HOG000283506
InParanoidⁱ	P02930
KOⁱ	K12340
OMAⁱ	YNAKQQL
PhylomeDBⁱ	P02930

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11009-MONOMER MetaCyc:EG11009-MONOMER

BioCycⁱ

EcoCyc:EG11009-MONOMER
MetaCyc:EG11009-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P02930
Protein Ontology More...PROⁱ	PR:P02930

Family and domain databases

InterProⁱ	View protein in InterPro IPR003423 OMP_efflux IPR010130 T1SS_OMP_TolC
Pfamⁱ	View protein in Pfam PF02321 OEP, 2 hits
TIGRFAMsⁱ	TIGR01844 type_I_sec_TolC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TOLC_ECOLI
Accessionⁱ	P02930Primary (citable) accession number: P02930 Secondary accession number(s): Q2M9G5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	June 27, 2006
	Last modified:	September 12, 2018
	This is version 176 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P02930 (TOLC_ECOLI)

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Outer membrane protein TolC

tolC

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ