GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ECOLI:OMPF

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ompF (synonyms: cmlB, coa, cry, tolF)
Protein Name(s) Outer membrane protein F

Outer membrane protein 1A Outer membrane protein B Outer membrane protein IA Porin OmpF

External Links
UniProt P02931
EMBL J01655
U00096
AP009048
PIR A93449
RefSeq NP_415449.1
YP_489201.1
PDB 1BT9
1GFM
1GFN
1GFO
1GFP
1GFQ
1HXT
1HXU
1HXX
1MPF
1OPF
2OMF
2ZFG
2ZLD
3FYX
3HW9
3HWB
3K19
3K1B
3POQ
3POU
3POX
4GCP
4GCQ
4GCS
4JFB
4LSE
4LSF
4LSH
4LSI
PDBsum 1BT9
1GFM
1GFN
1GFO
1GFP
1GFQ
1HXT
1HXU
1HXX
1MPF
1OPF
2OMF
2ZFG
2ZLD
3FYX
3HW9
3HWB
3K19
3K1B
3POQ
3POU
3POX
4GCP
4GCQ
4GCS
4JFB
4LSE
4LSF
4LSH
4LSI
ProteinModelPortal P02931
SMR P02931
DIP DIP-10398N
IntAct P02931
MINT MINT-1511804
STRING 511145.b0929
TCDB 1.B.1.1.1
SWISS-2DPAGE P02931
PaxDb P02931
PRIDE P02931
EnsemblBacteria AAC74015
BAA35675
GeneID 12931024
945554
KEGG ecj:Y75_p0901
eco:b0929
PATRIC 32117073
EchoBASE EB0665
EcoGene EG10671
eggNOG COG3203
HOGENOM HOG000272406
InParanoid P02931
KO K09476
OMA YAINQID
OrthoDB EOG65J4ZQ
PhylomeDB P02931
BioCyc EcoCyc:EG10671-MONOMER
ECOL316407:JW0912-MONOMER
MetaCyc:EG10671-MONOMER
EvolutionaryTrace P02931
PRO PR:P02931
Proteomes UP000000318
UP000000625
Genevestigator P02931
GO GO:0009279
GO:0046930
GO:0042912
GO:0015238
GO:0015075
GO:0015288
GO:0043213
GO:0006855
GO:0034220
Gene3D 2.40.160.10
InterPro IPR023614
IPR001897
IPR001702
IPR013793
Pfam PF00267
PRINTS PR00183
PR00182
PROSITE PS00576

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009279

cell outer membrane

PMID:10806384[1]

ECO:0000314

C

Table 1

complete

part_of

GO:0034702

ion channel complex

PMID:15465872[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0047485

protein N-terminus binding

PMID:15465872[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P08083

F

Seeded From UniProt

complete

enables

GO:0097718

disordered domain specific binding

PMID:15465872[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00646

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:15465872[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0070207

protein homotrimerization

PMID:15465872[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:15465872[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005216

ion channel activity

PMID:15465872[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0034220

ion transmembrane transport

PMID:15465872[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

GO:0015288

porin activity

PMID:8702816[3]

ECO:0000315

F

Figure 3 shows the differing growth rate of wild-type and OmpF mutants when grown on maltotriose and maltooligosaccharides. The N-terminal mutations allow for growth on carbon sources larger than the normal exclusion limit.

complete
CACAO 10074

enables

GO:0042802

identical protein binding

PMID:8590000[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02931

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:8589999[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02931

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:23201272[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02931

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21098297[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02931

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18334212[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02931

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16079137[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02931

F

Seeded From UniProt

complete

enables

GO:0015288

porin activity

PMID:8702817[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0046930

pore complex

PMID:1380671[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042912

colicin transmembrane transporter activity

PMID:1706457[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0015238

drug transmembrane transporter activity

PMID:7044293[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:338582[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:22534293[15]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:17309111[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:15911532[17]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:10806384[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006855

drug transmembrane transport

PMID:7044293[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043213

bacteriocin transport

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0042912

P

Seeded From UniProt

complete

enables

GO:0015288

porin activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001702
InterPro:IPR001897
InterPro:IPR033900

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001702
InterPro:IPR001897
InterPro:IPR033900

C

Seeded From UniProt

complete

involved_in

GO:0055085

transmembrane transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001702
InterPro:IPR001897

P

Seeded From UniProt

complete

involved_in

GO:0034220

ion transmembrane transport

PMID:2580220[18]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0015288

porin activity

PMID:2580220[18]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0015075

ion transmembrane transporter activity

PMID:2580220[18]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0998
UniProtKB-SubCell:SL-0040

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

involved_in

GO:0006811

ion transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0406

P

Seeded From UniProt

complete

enables

GO:0015288

porin activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0626

F

Seeded From UniProt

complete

part_of

GO:0046930

pore complex

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0626

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Molloy, MP et al. (2000) Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 267 2871-81 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 Zakharov, SD et al. (2004) Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import. Biophys. J. 87 3901-11 PubMed GONUTS page
  3. ↑ Lou, KL et al. (1996) Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis. J. Biol. Chem. 271 20669-75 PubMed GONUTS page
  4. ↑ Pebay-Peyroula, E et al. (1995) Detergent structure in tetragonal crystals of OmpF porin. Structure 3 1051-9 PubMed GONUTS page
  5. ↑ Cowan, SW et al. (1995) The structure of OmpF porin in a tetragonal crystal form. Structure 3 1041-50 PubMed GONUTS page
  6. ↑ Ziervogel, BK & Roux, B (2013) The binding of antibiotics in OmpF porin. Structure 21 76-87 PubMed GONUTS page
  7. ↑ Housden, NG et al. (2010) Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF. Proc. Natl. Acad. Sci. U.S.A. 107 21412-7 PubMed GONUTS page
  8. ↑ Baboolal, TG et al. (2008) Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F. Structure 16 371-9 PubMed GONUTS page
  9. ↑ Stenberg, F et al. (2005) Protein complexes of the Escherichia coli cell envelope. J. Biol. Chem. 280 34409-19 PubMed GONUTS page
  10. ↑ Saint, N et al. (1996) Structural and functional characterization of OmpF porin mutants selected for larger pore size. II. Functional characterization. J. Biol. Chem. 271 20676-80 PubMed GONUTS page
  11. ↑ Cowan, SW et al. (1992) Crystal structures explain functional properties of two E. coli porins. Nature 358 727-33 PubMed GONUTS page
  12. ↑ Bourdineaud, JP et al. (1990) Involvement of OmpF during reception and translocation steps of colicin N entry. Mol. Microbiol. 4 1737-43 PubMed GONUTS page
  13. ↑ 13.0 13.1 Harder, KJ et al. (1981) Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin. Antimicrob. Agents Chemother. 20 549-52 PubMed GONUTS page
  14. ↑ Palva, ET & Randall, LL (1978) Arrangement of protein I in Escherichia coli outer membrane: cross-linking study. J. Bacteriol. 133 279-86 PubMed GONUTS page
  15. ↑ Han, MJ et al. (2012) Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains. J. Microbiol. Biotechnol. 22 470-8 PubMed GONUTS page
  16. ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
  17. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  18. ↑ 18.0 18.1 18.2 Nikaido, H & Vaara, M (1985) Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49 1-32 PubMed GONUTS page
Retrieved from "https://gowiki.tamu.edu/wiki/index.php?title=ECOLI:OMPF&oldid=5953479"