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1.B.1.1.1
OmpF general porin. OmpF can deliver peptides of >6 KDa (epitopes) including protamine, through the pore lumen from the periplasm to the outside (Housden et al., 2010; Ghale et al. 2014).  For cephalosporin antibiotics, the interaction strength series is ceftriaxone > cefpirome > ceftazidime (Lovelle et al. 2011).  An unfolded protein such as colicin E9 can thread through OmpF from the outside to reach the periplasm (Housden et al. 2013).  Polynucleotides can pass through OmpF (Hadi-Alijanvand and Rouhani 2015). LPS influences the movement of bulk ions (K+ and Cl-), but the ion selectivity of OmpF is mainly affected by bulk ion concentrations (Patel et al. 2016).  OMPs such as OmpF cluster into islands that restrict their lateral mobility, while IMPs generally diffuse throughout the cell. Rassam et al. 2018 demonstrated that when transient, energy-dependent transmembrane connections are formed, IMPs become subjugated by the inherent organisation of OMPs, and that such connections impact IMP function. They showed that while establishing a translocon for import, colicin ColE9 sequesters the IMPs of the proton motive force (PMF)-linked Tol-Pal complex into islands mirroring those of colicin-bound OMPs. Through this imposed organisation, the bacteriocin subverts the outer-membrane stabilizing role of Tol-Pal, blocking its recruitment to cell division sites and slowing membrane constriction. The ordering of IMPs by OMPs via an energised inter-membrane bridge represents an emerging functional paradigm in cell envelope biology (Rassam et al. 2018). Colicin E9 (ColE9) disordered regions exploit OmpF for direction-specific binding, which ensures the constrained presentation of an activating signal within the bacterial periplasm (Housden et al. 2018). Anionic lipid binding can prevent closure of OmpF channels, thereby increasing access of antibiotics that use porin-mediated pathways (Liko et al. 2018). OmpF may be the major route of D-lactate/D-3-hydroxybutyrate oligo-ester secretion (Utsunomia et al. 2017).

Accession Number:P02931
Protein Name:OMPF aka TOLF aka CMLB aka COA aka CRY aka B0929
Length:362
Molecular Weight:39333.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell outer membrane1 / Multi-pass membrane protein2
Substrate Ceftriaxone, Cefpirome, ions, peptides, Colicin E9, Protamine, Ceftazidime

Cross database links:

Genevestigator: P02931
EchoBASE: EB0665
EcoGene: EG10671
eggNOG: COG3203
HEGENOM: HBG673855
DIP: DIP-10398N
RefSeq: AP_001559.1    NP_415449.1   
Entrez Gene ID: 945554   
Pfam: PF00267   
Drugbank: Drugbank Link   
BioCyc: EcoCyc:EG10671-MONOMER    ECOL168927:B0929-MONOMER   
KEGG: ecj:JW0912    eco:b0929   

Gene Ontology

GO:0009279 C:cell outer membrane
GO:0005886 C:plasma membrane
GO:0046930 C:pore complex
GO:0015288 F:porin activity
GO:0009597 P:detection of virus
GO:0046718 P:entry of virus into host cell
GO:0006811 P:ion transport

References (13)

[1] “Primary structure of the ompF gene that codes for a major outer membrane protein of Escherichia coli K-12.”  Inokuchi K.et.al.   6294623
[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.et.al.   8905232
[3] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[5] “Amino acid sequence of the signal peptide of OmpF, a major outer membrane protein of Escherichia coli.”  Mutoh N.et.al.   7037455
[6] “Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r.”  Chen R.et.al.   7049161
[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.et.al.   2997131
[8] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[9] “Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis.”  Molloy M.P.et.al.   9629924
[10] “Protein complexes of the Escherichia coli cell envelope.”  Stenberg F.et.al.   16079137
[11] “Crystal structures explain functional properties of two E. coli porins.”  Cowan S.W.et.al.   1380671
[12] “Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli.”  Jeanteur D.et.al.   7524100
[13] “Stability of trimeric OmpF porin: the contributions of the latching loop L2.”  Phale P.S.et.al.   9843370
Structure:
1BT9   1GFM   1GFN   1GFO   1GFP   1GFQ   1HXT   1HXU   1HXX   1MPF   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MMKRNILAVI VPALLVAGTA NAAEIYNKDG NKVDLYGKAV GLHYFSKGNG ENSYGGNGDM 
61:	TYARLGFKGE TQINSDLTGY GQWEYNFQGN NSEGADAQTG NKTRLAFAGL KYADVGSFDY 
121:	GRNYGVVYDA LGYTDMLPEF GGDTAYSDDF FVGRVGGVAT YRNSNFFGLV DGLNFAVQYL 
181:	GKNERDTARR SNGDGVGGSI SYEYEGFGIV GAYGAADRTN LQEAQPLGNG KKAEQWATGL 
241:	KYDANNIYLA ANYGETRNAT PITNKFTNTS GFANKTQDVL LVAQYQFDFG LRPSIAYTKS 
301:	KAKDVEGIGD VDLVNYFEVG ATYYFNKNMS TYVDYIINQI DSDNKLGVGS DDTVAVGIVY 
361:	QF