P02931 · OMPF_ECOLI
- ProteinOuter membrane porin F
- GeneompF
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids362 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Forms pores that allow passive diffusion of small molecules across the outer membrane.
(Microbial infection) It is also a receptor for the bacteriophage T2. Is the major receptor for colicin E5 (Probable).
(Microbial infection) Probably translocates colicin E3 (and other A-type colicins) across the outer membrane (PubMed:18636093).
(Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536 (ECL_04451); polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Cellular Component | membrane | |
Cellular Component | monoatomic ion channel complex | |
Cellular Component | pore complex | |
Molecular Function | colicin transmembrane transporter activity | |
Molecular Function | disordered domain specific binding | |
Molecular Function | identical protein binding | |
Molecular Function | lipid binding | |
Molecular Function | lipopolysaccharide binding | |
Molecular Function | monoatomic ion channel activity | |
Molecular Function | porin activity | |
Biological Process | monoatomic ion transmembrane transport | |
Biological Process | protein homotrimerization | |
Biological Process | protein transport |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameOuter membrane porin F
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP02931
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell outer membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane, topological domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 23-28 | Beta stranded | ||||
Sequence: AEIYNK | ||||||
Topological domain | 29 | Periplasmic | ||||
Sequence: D | ||||||
Transmembrane | 30-45 | Beta stranded | ||||
Sequence: GNKVDLYGKAVGLHYF | ||||||
Topological domain | 46-60 | Extracellular | ||||
Sequence: SKGNGENSYGGNGDM | ||||||
Transmembrane | 61-73 | Beta stranded | ||||
Sequence: TYARLGFKGETQI | ||||||
Topological domain | 74-75 | Periplasmic | ||||
Sequence: NS | ||||||
Transmembrane | 76-88 | Beta stranded | ||||
Sequence: DLTGYGQWEYNFQ | ||||||
Topological domain | 89-104 | Extracellular | ||||
Sequence: GNNSEGADAQTGNKTR | ||||||
Transmembrane | 105-113 | Beta stranded | ||||
Sequence: LAFAGLKYA | ||||||
Topological domain | 114-115 | Periplasmic | ||||
Sequence: DV | ||||||
Transmembrane | 116-122 | Beta stranded | ||||
Sequence: GSFDYGR | ||||||
Topological domain | 123-156 | Extracellular | ||||
Sequence: NYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVG | ||||||
Transmembrane | 157-163 | Beta stranded | ||||
Sequence: GVATYRN | ||||||
Topological domain | 164-171 | Periplasmic | ||||
Sequence: SNFFGLVD | ||||||
Transmembrane | 172-181 | Beta stranded | ||||
Sequence: GLNFAVQYLG | ||||||
Topological domain | 182-193 | Extracellular | ||||
Sequence: KNERDTARRSNG | ||||||
Transmembrane | 194-204 | Beta stranded | ||||
Sequence: DGVGGSISYEY | ||||||
Topological domain | 205 | Periplasmic | ||||
Sequence: E | ||||||
Transmembrane | 206-217 | Beta stranded | ||||
Sequence: GFGIVGAYGAAD | ||||||
Topological domain | 218-232 | Extracellular | ||||
Sequence: RTNLQEAQPLGNGKK | ||||||
Transmembrane | 233-244 | Beta stranded | ||||
Sequence: AEQWATGLKYDA | ||||||
Topological domain | 245 | Periplasmic | ||||
Sequence: N | ||||||
Transmembrane | 246-257 | Beta stranded | ||||
Sequence: NIYLAANYGETR | ||||||
Topological domain | 258-274 | Extracellular | ||||
Sequence: NATPITNKFTNTSGFAN | ||||||
Transmembrane | 275-287 | Beta stranded | ||||
Sequence: KTQDVLLVAQYQF | ||||||
Topological domain | 288-289 | Periplasmic | ||||
Sequence: DF | ||||||
Transmembrane | 290-303 | Beta stranded | ||||
Sequence: GLRPSIAYTKSKAK | ||||||
Topological domain | 304-313 | Extracellular | ||||
Sequence: DVEGIGDVDL | ||||||
Transmembrane | 314-325 | Beta stranded | ||||
Sequence: VNYFEVGATYYF | ||||||
Topological domain | 326-327 | Periplasmic | ||||
Sequence: NK | ||||||
Transmembrane | 328-337 | Beta stranded | ||||
Sequence: NMSTYVDYII | ||||||
Topological domain | 338-352 | Extracellular | ||||
Sequence: NQIDSDNKLGVGSDD | ||||||
Transmembrane | 353-362 | Beta stranded | ||||
Sequence: TVAVGIVYQF |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Leads to decreased susceptibility to a number of hydrophilic antibiotics including ampicillin, cefoxitin and tetracycline (PubMed:19721064).
Deletion of ompF confers resistance to colicin E5 (PubMed:27723824).
Deletion of ompF confers resistance to colicin E5 (PubMed:27723824).
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 88 | in strain: B/r; AA sequence | ||||
Sequence: Q → E | ||||||
Natural variant | 139 | in strain: B/r; AA sequence | ||||
Sequence: E → G | ||||||
Natural variant | 284 | in strain: B/r; AA sequence | ||||
Sequence: Q → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
Miscellaneous
Chemistry
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MMKRNILAVIVPALLVAGTANA | ||||||
Chain | PRO_0000025237 | 23-362 | Outer membrane porin F | |||
Sequence: AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF |
Proteomic databases
Expression
Interaction
Subunit
Homotrimer (PubMed:16079137, PubMed:18636093, PubMed:2464593, PubMed:9843370).
Forms mixed heterotrimers with OmpC and with PhoE; other mixed heterotrimers are also probable (PubMed:2464593).
Forms mixed heterotrimers with OmpC and with PhoE; other mixed heterotrimers are also probable (PubMed:2464593).
(Microbial infection) Trimeric complexes with colicin E3, BtuB and OmpF can be cross-linked and immunoprecipitated (PubMed:18636093).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P02931 | cna P08083 | 3 | EBI-371336, EBI-15691934 | |
XENO | P02931 | col P09883 | 4 | EBI-371336, EBI-1029888 | |
BINARY | P02931 | mlaA P76506 | 4 | EBI-371336, EBI-1128511 | |
BINARY | P02931 | ompF P02931 | 7 | EBI-371336, EBI-371336 |
Protein-protein interaction databases
Structure
Family & Domains
Domain
Each subunit of the trimer has a water-filled pore with a narrow, elliptically shaped (7 X 11 Angstroms) selectivity filter which has a solvent accessible area of 30-40 Angstroms2 (PubMed:18636093).
Sequence similarities
Belongs to the Gram-negative porin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length362
- Mass (Da)39,333
- Last updated1986-07-21 v1
- Checksum3F0974D96DB65464
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J01655 EMBL· GenBank· DDBJ | AAA24244.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC74015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA35675.1 EMBL· GenBank· DDBJ | Genomic DNA |