UniProt functional annotation for P40710



	UniProt functional annotation for P40710

UniProt code: P40710.

Organism: Escherichia coli (strain K12).

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

Function: Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes (PubMed:7635807). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR (PubMed:7635808, PubMed:15252048). DegP induction seems to require membrane anchoring of this protein (PubMed:15252048). Structural changes and/or interaction of the CXXC motif with its environment may lead to activation of the Cpx stress response (PubMed:17698001). {ECO:0000269|PubMed:11830644, ECO:0000269|PubMed:15252048, ECO:0000269|PubMed:17698001, ECO:0000269|PubMed:7635808}.

Subunit: Probably exists as a monomer in vivo, can however form homodimers which swap domains (PubMed:17698001). {ECO:0000269|PubMed:17698001}.

Subcellular location: Cell outer membrane {ECO:0000269|PubMed:15252048, ECO:0000305|PubMed:7635808}; Lipid-anchor {ECO:0000305|PubMed:15252048, ECO:0000305|PubMed:7635808}.

Domain: The mature protein has 2 domains, the N-terminus (residues 21- 100) and the C-terminus (residues 126-236) joined by a flexible linker; both domains form beta-barrels. In the crystal structure of the soluble mutant (Ala-21) the N-terminus of 1 subunit interacts with the C- terminus of the other. {ECO:0000269|PubMed:17698001}.

Ptm: Palmitoylated. {ECO:0000269|PubMed:7635808}.

Ptm: Seems to only form a disulfide bond between Cys-165 and Cys-231. The 2 other cysteine residues may however be chemically active. {ECO:0000269|Ref.4}.

Disruption phenotype: No visible phenotype (PubMed:7635808). Slightly copper sensitive (PubMed:7635807). Decreased numbers of stationary phase cells bind to hydrophobic surfaces, cellular adhesion has altered dynamic properties; no induction of cpxR when cells bind to hydrophobic surfaces (PubMed:11830644). {ECO:0000269|PubMed:11830644, ECO:0000269|PubMed:7635807, ECO:0000269|PubMed:7635808}.

Annotations taken from UniProtKB at the EBI.


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



Function:		Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes (PubMed:7635807). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR (PubMed:7635808, PubMed:15252048). DegP induction seems to require membrane anchoring of this protein (PubMed:15252048). Structural changes and/or interaction of the CXXC motif with its environment may lead to activation of the Cpx stress response (PubMed:17698001). {ECO:0000269\|PubMed:11830644, ECO:0000269\|PubMed:15252048, ECO:0000269\|PubMed:17698001, ECO:0000269\|PubMed:7635808}.


Subunit:		Probably exists as a monomer in vivo, can however form homodimers which swap domains (PubMed:17698001). {ECO:0000269\|PubMed:17698001}.
Subcellular location:		Cell outer membrane {ECO:0000269\|PubMed:15252048, ECO:0000305\|PubMed:7635808}; Lipid-anchor {ECO:0000305\|PubMed:15252048, ECO:0000305\|PubMed:7635808}.
Domain:		The mature protein has 2 domains, the N-terminus (residues 21- 100) and the C-terminus (residues 126-236) joined by a flexible linker; both domains form beta-barrels. In the crystal structure of the soluble mutant (Ala-21) the N-terminus of 1 subunit interacts with the C- terminus of the other. {ECO:0000269\|PubMed:17698001}.
Ptm:		Palmitoylated. {ECO:0000269\|PubMed:7635808}.
Ptm:		Seems to only form a disulfide bond between Cys-165 and Cys-231. The 2 other cysteine residues may however be chemically active. {ECO:0000269\|Ref.4}.
Disruption phenotype:		No visible phenotype (PubMed:7635808). Slightly copper sensitive (PubMed:7635807). Decreased numbers of stationary phase cells bind to hydrophobic surfaces, cellular adhesion has altered dynamic properties; no induction of cpxR when cells bind to hydrophobic surfaces (PubMed:11830644). {ECO:0000269\|PubMed:11830644, ECO:0000269\|PubMed:7635807, ECO:0000269\|PubMed:7635808}.