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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10671. ompF.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 286Beta stranded
Topological domaini29 – 291Periplasmic
Transmembranei30 – 4516Beta strandedAdd
BLAST
Topological domaini46 – 6015ExtracellularAdd
BLAST
Transmembranei61 – 7313Beta strandedAdd
BLAST
Topological domaini74 – 752Periplasmic
Transmembranei76 – 8813Beta strandedAdd
BLAST
Topological domaini89 – 10416ExtracellularAdd
BLAST
Transmembranei105 – 1139Beta stranded
Topological domaini114 – 1152Periplasmic
Transmembranei116 – 1227Beta stranded
Topological domaini123 – 15634ExtracellularAdd
BLAST
Transmembranei157 – 1637Beta stranded
Topological domaini164 – 1718Periplasmic
Transmembranei172 – 18110Beta stranded
Topological domaini182 – 19312ExtracellularAdd
BLAST
Transmembranei194 – 20411Beta strandedAdd
BLAST
Topological domaini205 – 2051Periplasmic
Transmembranei206 – 21712Beta strandedAdd
BLAST
Topological domaini218 – 23215ExtracellularAdd
BLAST
Transmembranei233 – 24412Beta strandedAdd
BLAST
Topological domaini245 – 2451Periplasmic
Transmembranei246 – 25712Beta strandedAdd
BLAST
Topological domaini258 – 27417ExtracellularAdd
BLAST
Transmembranei275 – 28713Beta strandedAdd
BLAST
Topological domaini288 – 2892Periplasmic
Transmembranei290 – 30314Beta strandedAdd
BLAST
Topological domaini304 – 31310Extracellular
Transmembranei314 – 32512Beta strandedAdd
BLAST
Topological domaini326 – 3272Periplasmic
Transmembranei328 – 33710Beta stranded
Topological domaini338 – 35215ExtracellularAdd
BLAST
Transmembranei353 – 36210Beta stranded

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22223 PublicationsAdd
BLAST
Chaini23 – 362340Outer membrane protein FPRO_0000025237Add
BLAST

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 interactions.
DIPiDIP-10398N.
IntActiP02931. 5 interactions.
MINTiMINT-1511804.
STRINGi511145.b0929.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 285Combined sources
Beta strandi31 – 4515Combined sources
Beta strandi47 – 504Combined sources
Beta strandi53 – 553Combined sources
Beta strandi57 – 593Combined sources
Beta strandi62 – 7211Combined sources
Beta strandi74 – 9118Combined sources
Turni95 – 1006Combined sources
Beta strandi102 – 11211Combined sources
Turni113 – 1153Combined sources
Beta strandi116 – 1249Combined sources
Helixi128 – 1314Combined sources
Turni132 – 1343Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi152 – 16413Combined sources
Helixi165 – 1684Combined sources
Beta strandi173 – 1808Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi195 – 20410Combined sources
Beta strandi207 – 21711Combined sources
Helixi220 – 2234Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi231 – 24414Combined sources
Beta strandi247 – 25812Combined sources
Beta strandi260 – 2645Combined sources
Turni265 – 2684Combined sources
Beta strandi269 – 2724Combined sources
Beta strandi274 – 28512Combined sources
Beta strandi290 – 30516Combined sources
Turni306 – 3083Combined sources
Beta strandi309 – 32618Combined sources
Beta strandi329 – 33810Combined sources
Beta strandi353 – 36210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 30-362.
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.
OrthoDBiEOG65J4ZQ.
PhylomeDBiP02931.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881Q → E AA sequence (PubMed:7049161).Curated
Sequence conflicti139 – 1391E → G AA sequence (PubMed:7049161).Curated
Sequence conflicti284 – 2841Q → L AA sequence (PubMed:7049161).Curated

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
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. Positions 30-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260018. 305 interactions.
DIPiDIP-10398N.
IntActiP02931. 5 interactions.
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.
OrthoDBiEOG65J4ZQ.
PhylomeDBiP02931.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP02931.
PROiP02931.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the ompF gene that codes for a major outer membrane protein of Escherichia coli K-12."
    Inokuchi K., Mutoh N., Matsuyama S., Mizushima S.
    Nucleic Acids Res. 10:6957-6968(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Amino acid sequence of the signal peptide of OmpF, a major outer membrane protein of Escherichia coli."
    Mutoh N., Inokuchi K., Mizushima S.
    FEBS Lett. 137:171-174(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
  6. "Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r."
    Chen R., Kramer C., Schmidmayr W., Chen-Schmeisser U., Henning U.
    Biochem. J. 203:33-43(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-362.
  7. "Construction of a series of ompF-ompC chimeric genes by in vivo homologous recombination in Escherichia coli and characterization of the translational products."
    Nogami T., Mizuno T., Mizushima S.
    J. Bacteriol. 164:797-801(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-63.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-34 AND 39-47.
    Strain: K12 / EMG2.
  9. "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
    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.
    Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-27.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  12. "Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli."
    Duval V., Nicoloff H., Levy S.B.
    Antimicrob. Agents Chemother. 53:4944-4948(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN ANTIBIOTIC SUSCEPTIBILITY, INDUCTION, REGULATION BY LON/YCGE, DISRUPTION PHENOTYPE.
    Strain: K12 / AG100.
  13. "Crystal structures explain functional properties of two E. coli porins."
    Cowan S.W., Schirmer T., Rummel G., Steiert M., Ghosh R., Pauptit R.A., Jansonius J.N., Rosenbusch J.P.
    Nature 358:727-733(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  14. "Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli."
    Jeanteur D., Schirmer T., Fourel D., Simonet V., Rummel G., Widmer C., Rosenbusch J.P., Pattus F., Pages J.-M.
    Proc. Natl. Acad. Sci. U.S.A. 91:10675-10679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT ASP-141.
  15. "Stability of trimeric OmpF porin: the contributions of the latching loop L2."
    Phale P.S., Philippsen A., Kiefhaber T., Koebnik R., Phale V.P., Schirmer T., Rosenbusch J.P.
    Biochemistry 37:15663-15670(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

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: July 6, 2016
This is version 171 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.