UniProt functional annotation for P06996



	UniProt functional annotation for P06996

UniProt code: P06996.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.

Function: (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF. {ECO:0000305|PubMed:27723824}.

Function: (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity. {ECO:0000269|PubMed:27723824}.

Subunit: Homotrimer (PubMed:2464593, PubMed:16949612). Forms mixed heterotrimers with OmpF and with PhoE; other mixed heterotrimers are also probable (PubMed:2464593). {ECO:0000269|PubMed:16949612, ECO:0000269|PubMed:2464593}.

Subcellular location: Cell outer membrane {ECO:0000269|PubMed:2464593}; Multi-pass membrane protein {ECO:0000269|PubMed:16949612}.

Induction: By growth in high osmolarity conditions (high sugar or salt) under control of OmpR (at protein level) (PubMed:3010044, PubMed:2464593). In the presence of 0.2 M NaCl, 2.0 mM sodium cholate (bile salts) decreases expression from the ompC promoter; how this is mediated is unknown (PubMed:28423182). {ECO:0000269|PubMed:2464593, ECO:0000269|PubMed:28423182, ECO:0000269|PubMed:3010044}.

Domain: Loop L3 (residues 116-133) extends along the inner side of the beta barrel wall and may constrict the pore mid-length. {ECO:0000269|PubMed:16949612}.

Disruption phenotype: Deletion of both ompC and ompF confers resistance to colicin E5 and to the toxic activity of CdiA-EC536. {ECO:0000269|PubMed:27723824}.

Miscellaneous: Binds 1 Mg(2+) per subunit; could be Ca(2+) in vivo.

Similarity: Belongs to the Gram-negative porin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Forms pores that allow passive diffusion of small molecules across the outer membrane.



Function:		(Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF. {ECO:0000305\|PubMed:27723824}.



Function:		(Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity. {ECO:0000269\|PubMed:27723824}.


Subunit:		Homotrimer (PubMed:2464593, PubMed:16949612). Forms mixed heterotrimers with OmpF and with PhoE; other mixed heterotrimers are also probable (PubMed:2464593). {ECO:0000269\|PubMed:16949612, ECO:0000269\|PubMed:2464593}.
Subcellular location:		Cell outer membrane {ECO:0000269\|PubMed:2464593}; Multi-pass membrane protein {ECO:0000269\|PubMed:16949612}.
Induction:		By growth in high osmolarity conditions (high sugar or salt) under control of OmpR (at protein level) (PubMed:3010044, PubMed:2464593). In the presence of 0.2 M NaCl, 2.0 mM sodium cholate (bile salts) decreases expression from the ompC promoter; how this is mediated is unknown (PubMed:28423182). {ECO:0000269\|PubMed:2464593, ECO:0000269\|PubMed:28423182, ECO:0000269\|PubMed:3010044}.
Domain:		Loop L3 (residues 116-133) extends along the inner side of the beta barrel wall and may constrict the pore mid-length. {ECO:0000269\|PubMed:16949612}.
Disruption phenotype:		Deletion of both ompC and ompF confers resistance to colicin E5 and to the toxic activity of CdiA-EC536. {ECO:0000269\|PubMed:27723824}.
Miscellaneous:		Binds 1 Mg(2+) per subunit; could be Ca(2+) in vivo.
Similarity:		Belongs to the Gram-negative porin family. {ECO:0000305}.