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Reviewed, UniProtKB/Swiss-Prot P02931 (OMPF_ECOLI)

Last modified June 16, 2009. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Outer membrane protein F
Alternative name(s):
    Porin ompF
    Outer membrane protein 1A
    Outer membrane protein IA
    Outer membrane protein B
Gene names
Name: ompF
Synonyms: cmlB, coa, cry, tolF
Ordered Locus Names: b0929, JW0912
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2.

Subunit structure

Homotrimer. Ref.10

Subcellular location

Cell outer membrane; Multi-pass membrane protein. Ref.10

Sequence similarities

Belongs to the Gram-negative porin family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.6 Ref.8 Ref.9
Chain23 – 362340Outer membrane protein F
PRO_0000025237

Regions

Transmembrane23 – 286
Topological domain291Periplasmic
Transmembrane30 – 4516
Topological domain46 – 6015Extracellular
Transmembrane61 – 7313
Topological domain74 – 752Periplasmic
Transmembrane76 – 8813
Topological domain89 – 10416Extracellular
Transmembrane105 – 1139
Topological domain114 – 1152Periplasmic
Transmembrane116 – 1227
Topological domain123 – 15634Extracellular
Transmembrane157 – 1637
Topological domain164 – 1718Periplasmic
Transmembrane172 – 18110
Topological domain182 – 19312Extracellular
Transmembrane194 – 20411
Topological domain2051Periplasmic
Transmembrane206 – 21712
Topological domain218 – 23215Extracellular
Transmembrane233 – 24412
Topological domain2451Periplasmic
Transmembrane246 – 25712
Topological domain258 – 27417Extracellular
Transmembrane275 – 28713
Topological domain288 – 2892Periplasmic
Transmembrane290 – 30314
Topological domain304 – 31310Extracellular
Transmembrane314 – 32512
Topological domain326 – 3272Periplasmic
Transmembrane328 – 33710
Topological domain338 – 35215Extracellular
Transmembrane353 – 36210

Experimental info

Sequence conflict881Q → E AA sequence Ref.6
Sequence conflict1391E → G AA sequence Ref.6
Sequence conflict2841Q → L AA sequence Ref.6

Secondary structure

1 ...................................................... 362
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P02931-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3F0974D96DB65464

FASTA36239,333
        10         20         30         40         50         60 
MMKRNILAVI VPALLVAGTA NAAEIYNKDG NKVDLYGKAV GLHYFSKGNG ENSYGGNGDM 

        70         80         90        100        110        120 
TYARLGFKGE TQINSDLTGY GQWEYNFQGN NSEGADAQTG NKTRLAFAGL KYADVGSFDY 

       130        140        150        160        170        180 
GRNYGVVYDA LGYTDMLPEF GGDTAYSDDF FVGRVGGVAT YRNSNFFGLV DGLNFAVQYL 

       190        200        210        220        230        240 
GKNERDTARR SNGDGVGGSI SYEYEGFGIV GAYGAADRTN LQEAQPLGNG KKAEQWATGL 

       250        260        270        280        290        300 
KYDANNIYLA ANYGETRNAT PITNKFTNTS GFANKTQDVL LVAQYQFDFG LRPSIAYTKS 

       310        320        330        340        350        360 
KAKDVEGIGD VDLVNYFEVG ATYYFNKNMS TYVDYIINQI DSDNKLGVGS DDTVAVGIVY 


QF

« Hide

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References

« Hide 'large scale' references
[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: 6294623] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 7037455] [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: 7049161] [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: 2997131] [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: 9298646] [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: 9629924] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-27.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]"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: 16079137] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[11]"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: 1380671] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[12]"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: 7524100] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT ASP-141.
[13]"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: 9843370] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

J01655 Genomic DNA. Translation: AAA24244.1.
U00096 Genomic DNA. Translation: AAC74015.1.
AP009048 Genomic DNA. Translation: BAA35675.1.
PIRMMECF. A93449.
RefSeqAP_001559.1.
NP_415449.1.

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:10398N.

Protein family/group databases

TCDB1.B.1.1.1. general bacterial porin (GBP) family.

2-D gel databases

SWISS-2DPAGEP02931.
2DBase-EcoliP02931.
ECO2DBASEB036.0. 6TH EDITION.

Proteomic databases

PRIDEP02931.

Genome annotation databases

GeneID945554.
GenomeReviewsGene locus JW0912 in contig AP009048_GR.
Gene locus b0929 in contig U00096_GR.
KEGGecj:JW0912.
eco:b0929.

Organism-specific databases

EchoBASEEB0665.
EcoGeneEG10671. ompF.
CMRSearch...

Phylogenomic databases

HOGENOMP02931.
OMAP02931. TIMYVEA.

Enzyme and pathway databases

BioCycEcoCyc:EG10671-MON.

Family and domain databases

InterProIPR001897. Porin_bac.
IPR013793. Porin_general_Gram-ve_CS.
IPR001702. Porin_Gram-ve.
[Graphical view]
Gene3DG3DSA:2.40.160.10. Porin_Gram-ve. 1 hit.
PfamPF00267. Porin_1. 1 hit.
[Graphical view]
PRINTSPR00183. ECOLIPORIN.
PR00182. ECOLNEIPORIN.
PROSITEPS00576. GRAM_NEG_PORIN. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameOMPF_ECOLI
AccessionPrimary (citable) accession number: P02931
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents