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Protein

Outer membrane protein F

Gene

ompF

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

Functioni

Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.1 Publication

GO - Molecular functioni

  • colicin transmembrane transporter activity Source: EcoCyc
  • drug transmembrane transporter activity Source: EcoCyc
  • ion transmembrane transporter activity Source: EcoCyc
  • porin activity Source: EcoliWiki

GO - Biological processi

  • drug transmembrane transport Source: EcoCyc
  • ion transmembrane transport Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Porin

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG10671-MONOMER.
ECOL316407:JW0912-MONOMER.
MetaCyc:EG10671-MONOMER.

Protein family/group databases

TCDBi1.B.1.1.1. the general bacterial porin (gbp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Outer membrane protein F
Alternative name(s):
Outer membrane protein 1A
Outer membrane protein B
Outer membrane protein IA
Porin OmpF
Gene namesi
Name:ompF
Synonyms:cmlB, coa, cry, tolF
Ordered Locus Names:b0929, JW0912
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10671. ompF.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei23 – 28Beta stranded6
Topological domaini29Periplasmic1
Transmembranei30 – 45Beta strandedAdd BLAST16
Topological domaini46 – 60ExtracellularAdd BLAST15
Transmembranei61 – 73Beta strandedAdd BLAST13
Topological domaini74 – 75Periplasmic2
Transmembranei76 – 88Beta strandedAdd BLAST13
Topological domaini89 – 104ExtracellularAdd BLAST16
Transmembranei105 – 113Beta stranded9
Topological domaini114 – 115Periplasmic2
Transmembranei116 – 122Beta stranded7
Topological domaini123 – 156ExtracellularAdd BLAST34
Transmembranei157 – 163Beta stranded7
Topological domaini164 – 171Periplasmic8
Transmembranei172 – 181Beta stranded10
Topological domaini182 – 193ExtracellularAdd BLAST12
Transmembranei194 – 204Beta strandedAdd BLAST11
Topological domaini205Periplasmic1
Transmembranei206 – 217Beta strandedAdd BLAST12
Topological domaini218 – 232ExtracellularAdd BLAST15
Transmembranei233 – 244Beta strandedAdd BLAST12
Topological domaini245Periplasmic1
Transmembranei246 – 257Beta strandedAdd BLAST12
Topological domaini258 – 274ExtracellularAdd BLAST17
Transmembranei275 – 287Beta strandedAdd BLAST13
Topological domaini288 – 289Periplasmic2
Transmembranei290 – 303Beta strandedAdd BLAST14
Topological domaini304 – 313Extracellular10
Transmembranei314 – 325Beta strandedAdd BLAST12
Topological domaini326 – 327Periplasmic2
Transmembranei328 – 337Beta stranded10
Topological domaini338 – 352ExtracellularAdd BLAST15
Transmembranei353 – 362Beta stranded10

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • pore complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Leads to decreased susceptibility to a number of hydrophilic antibiotics including ampicillin, cefoxitin and tetracycline.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 223 PublicationsAdd BLAST22
ChainiPRO_000002523723 – 362Outer membrane protein FAdd BLAST340

Proteomic databases

EPDiP02931.
PaxDbiP02931.
PRIDEiP02931.

2D gel databases

SWISS-2DPAGEP02931.

Expressioni

Inductioni

Levels of OmpF protein decrease in a lon/ycgE double disruption (at protein level).1 Publication

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi4260018. 305 interactors.
DIPiDIP-10398N.
IntActiP02931. 5 interactors.
MINTiMINT-1511804.
STRINGi511145.b0929.

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 28Combined sources5
Beta strandi31 – 45Combined sources15
Beta strandi47 – 50Combined sources4
Beta strandi53 – 55Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi62 – 72Combined sources11
Beta strandi74 – 91Combined sources18
Turni95 – 100Combined sources6
Beta strandi102 – 112Combined sources11
Turni113 – 115Combined sources3
Beta strandi116 – 124Combined sources9
Helixi128 – 131Combined sources4
Turni132 – 134Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi147 – 149Combined sources3
Beta strandi152 – 164Combined sources13
Helixi165 – 168Combined sources4
Beta strandi173 – 180Combined sources8
Beta strandi186 – 188Combined sources3
Beta strandi195 – 204Combined sources10
Beta strandi207 – 217Combined sources11
Helixi220 – 223Combined sources4
Beta strandi225 – 227Combined sources3
Beta strandi231 – 244Combined sources14
Beta strandi247 – 258Combined sources12
Beta strandi260 – 264Combined sources5
Turni265 – 268Combined sources4
Beta strandi269 – 272Combined sources4
Beta strandi274 – 285Combined sources12
Beta strandi290 – 305Combined sources16
Turni306 – 308Combined sources3
Beta strandi309 – 326Combined sources18
Beta strandi329 – 338Combined sources10
Beta strandi353 – 362Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BT9X-ray3.00A23-362[»]
1GFMX-ray3.50A23-362[»]
1GFNX-ray3.10A23-362[»]
1GFOX-ray3.30A23-362[»]
1GFPX-ray2.70A23-362[»]
1GFQX-ray2.80A23-362[»]
1HXTX-ray2.40A23-362[»]
1HXUX-ray3.00A23-362[»]
1HXXX-ray2.20A23-362[»]
1MPFX-ray3.00A23-362[»]
1OPFX-ray3.20A/B/C/D/E/F23-362[»]
2OMFX-ray2.40A23-362[»]
2ZFGX-ray1.59A23-362[»]
2ZLDX-ray3.00A/B23-362[»]
3FYXX-ray3.40A23-362[»]
3HW9X-ray2.61A/B1-362[»]
3HWBX-ray3.00A/B1-362[»]
3K19X-ray3.79A/B/C/D/E/F/G/H/I/J/K/L23-362[»]
3K1BX-ray4.39A/B/C/D23-362[»]
3O0EX-ray3.01A/B/C/D/E/F23-362[»]
3POQX-ray1.90A23-362[»]
3POUX-ray2.80A23-362[»]
3POXX-ray2.00A/B/C/D/E/F23-362[»]
4D5UX-ray3.50A/B/C/D/E/F23-362[»]
4GCPX-ray1.98A/B23-362[»]
4GCQX-ray2.20A/B23-362[»]
4GCSX-ray1.87A/B23-362[»]
4JFBX-ray3.80A/B/C/D/E/F23-362[»]
4LSEX-ray2.10A/B/C23-362[»]
4LSFX-ray1.90A/B23-362[»]
4LSHX-ray2.20A/B23-362[»]
4LSIX-ray2.09A/B/C23-362[»]
ProteinModelPortaliP02931.
SMRiP02931.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02931.

Family & Domainsi

Sequence similaritiesi

Belongs to the Gram-negative porin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105FCK. Bacteria.
COG3203. LUCA.
HOGENOMiHOG000272406.
InParanoidiP02931.
KOiK09476.
OMAiYAINQID.
PhylomeDBiP02931.

Family and domain databases

CDDicd00342. gram_neg_porins. 1 hit.
Gene3Di2.40.160.10. 1 hit.
InterProiIPR033900. Gram_neg_porin_domain.
IPR023614. Porin_dom.
IPR001897. Porin_gammaproteobac.
IPR001702. Porin_Gram-ve.
IPR013793. Porin_Gram-ve_CS.
[Graphical view]
PfamiPF00267. Porin_1. 1 hit.
[Graphical view]
PRINTSiPR00183. ECOLIPORIN.
PR00182. ECOLNEIPORIN.
PROSITEiPS00576. GRAM_NEG_PORIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02931-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKRNILAVI VPALLVAGTA NAAEIYNKDG NKVDLYGKAV GLHYFSKGNG
60 70 80 90 100
ENSYGGNGDM TYARLGFKGE TQINSDLTGY GQWEYNFQGN NSEGADAQTG
110 120 130 140 150
NKTRLAFAGL KYADVGSFDY GRNYGVVYDA LGYTDMLPEF GGDTAYSDDF
160 170 180 190 200
FVGRVGGVAT YRNSNFFGLV DGLNFAVQYL GKNERDTARR SNGDGVGGSI
210 220 230 240 250
SYEYEGFGIV GAYGAADRTN LQEAQPLGNG KKAEQWATGL KYDANNIYLA
260 270 280 290 300
ANYGETRNAT PITNKFTNTS GFANKTQDVL LVAQYQFDFG LRPSIAYTKS
310 320 330 340 350
KAKDVEGIGD VDLVNYFEVG ATYYFNKNMS TYVDYIINQI DSDNKLGVGS
360
DDTVAVGIVY QF
Length:362
Mass (Da):39,333
Last modified:July 21, 1986 - v1
Checksum:i3F0974D96DB65464
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti88Q → E AA sequence (PubMed:7049161).Curated1
Sequence conflicti139E → G AA sequence (PubMed:7049161).Curated1
Sequence conflicti284Q → L AA sequence (PubMed:7049161).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01655 Genomic DNA. Translation: AAA24244.1.
U00096 Genomic DNA. Translation: AAC74015.1.
AP009048 Genomic DNA. Translation: BAA35675.1.
PIRiA93449. MMECF.
RefSeqiNP_415449.1. NC_000913.3.
WP_000977920.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74015; AAC74015; b0929.
BAA35675; BAA35675; BAA35675.
GeneIDi945554.
KEGGiecj:JW0912.
eco:b0929.
PATRICi32117073. VBIEscCol129921_0961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01655 Genomic DNA. Translation: AAA24244.1.
U00096 Genomic DNA. Translation: AAC74015.1.
AP009048 Genomic DNA. Translation: BAA35675.1.
PIRiA93449. MMECF.
RefSeqiNP_415449.1. NC_000913.3.
WP_000977920.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BT9X-ray3.00A23-362[»]
1GFMX-ray3.50A23-362[»]
1GFNX-ray3.10A23-362[»]
1GFOX-ray3.30A23-362[»]
1GFPX-ray2.70A23-362[»]
1GFQX-ray2.80A23-362[»]
1HXTX-ray2.40A23-362[»]
1HXUX-ray3.00A23-362[»]
1HXXX-ray2.20A23-362[»]
1MPFX-ray3.00A23-362[»]
1OPFX-ray3.20A/B/C/D/E/F23-362[»]
2OMFX-ray2.40A23-362[»]
2ZFGX-ray1.59A23-362[»]
2ZLDX-ray3.00A/B23-362[»]
3FYXX-ray3.40A23-362[»]
3HW9X-ray2.61A/B1-362[»]
3HWBX-ray3.00A/B1-362[»]
3K19X-ray3.79A/B/C/D/E/F/G/H/I/J/K/L23-362[»]
3K1BX-ray4.39A/B/C/D23-362[»]
3O0EX-ray3.01A/B/C/D/E/F23-362[»]
3POQX-ray1.90A23-362[»]
3POUX-ray2.80A23-362[»]
3POXX-ray2.00A/B/C/D/E/F23-362[»]
4D5UX-ray3.50A/B/C/D/E/F23-362[»]
4GCPX-ray1.98A/B23-362[»]
4GCQX-ray2.20A/B23-362[»]
4GCSX-ray1.87A/B23-362[»]
4JFBX-ray3.80A/B/C/D/E/F23-362[»]
4LSEX-ray2.10A/B/C23-362[»]
4LSFX-ray1.90A/B23-362[»]
4LSHX-ray2.20A/B23-362[»]
4LSIX-ray2.09A/B/C23-362[»]
ProteinModelPortaliP02931.
SMRiP02931.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260018. 305 interactors.
DIPiDIP-10398N.
IntActiP02931. 5 interactors.
MINTiMINT-1511804.
STRINGi511145.b0929.

Protein family/group databases

TCDBi1.B.1.1.1. the general bacterial porin (gbp) family.

2D gel databases

SWISS-2DPAGEP02931.

Proteomic databases

EPDiP02931.
PaxDbiP02931.
PRIDEiP02931.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74015; AAC74015; b0929.
BAA35675; BAA35675; BAA35675.
GeneIDi945554.
KEGGiecj:JW0912.
eco:b0929.
PATRICi32117073. VBIEscCol129921_0961.

Organism-specific databases

EchoBASEiEB0665.
EcoGeneiEG10671. ompF.

Phylogenomic databases

eggNOGiENOG4105FCK. Bacteria.
COG3203. LUCA.
HOGENOMiHOG000272406.
InParanoidiP02931.
KOiK09476.
OMAiYAINQID.
PhylomeDBiP02931.

Enzyme and pathway databases

BioCyciEcoCyc:EG10671-MONOMER.
ECOL316407:JW0912-MONOMER.
MetaCyc:EG10671-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02931.
PROiP02931.

Family and domain databases

CDDicd00342. gram_neg_porins. 1 hit.
Gene3Di2.40.160.10. 1 hit.
InterProiIPR033900. Gram_neg_porin_domain.
IPR023614. Porin_dom.
IPR001897. Porin_gammaproteobac.
IPR001702. Porin_Gram-ve.
IPR013793. Porin_Gram-ve_CS.
[Graphical view]
PfamiPF00267. Porin_1. 1 hit.
[Graphical view]
PRINTSiPR00183. ECOLIPORIN.
PR00182. ECOLNEIPORIN.
PROSITEiPS00576. GRAM_NEG_PORIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOMPF_ECOLI
AccessioniPrimary (citable) accession number: P02931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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