UniProt functional annotation for P76541



	UniProt functional annotation for P76541

UniProt code: P76541.

Organism: Escherichia coli (strain K12).

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

Function: A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation (Probable). Two crystal forms have been seen; a form with a closed central pore that has 3 very small (1.1-2.2 Angstroms) channels per trimer lined by acidic and aromatic residues (PubMed:19451619, PubMed:20044574). A form with a large central pore (8-12 Angstroms) has also been seen; this is probably a functional pore which allows molecules to enter and exit the BMC in a selective, gated manner (PubMed:20851901, PubMed:20044574). Another group only sees the central pore in the presence of Zn(2+); soaking crystals in ZnCl(2) leads to dramatic conformational changes that open a central pore of about 12 Angstroms. Whether Zn(2+) binding is physiologically relevant is unclear, however it suggests a gating mechanism exists (PubMed:20851901). Ethanolamine-binding by the small channels has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (By similarity). {ECO:0000250|UniProtKB:Q8XLZ0, ECO:0000269|PubMed:19451619, ECO:0000269|PubMed:20044574, ECO:0000269|PubMed:20851901, ECO:0000305|PubMed:19451619, ECO:0000305|PubMed:20044574, ECO:0000305|PubMed:20851901, ECO:0007744|PDB:3GFH, ECO:0007744|PDB:3I82, ECO:0007744|PDB:3MPV}.

Pathway: Amine and polyamine degradation; ethanolamine degradation.

Subunit: Homotrimerizes to form a pseudohexamer (PubMed:19194002, PubMed:19451619, PubMed:20851901, PubMed:20044574). The trimers form a two-dimensional array about 37 Angstroms thick (PubMed:19451619, PubMed:20044574). {ECO:0000269|PubMed:19194002, ECO:0000269|PubMed:19451619, ECO:0000269|PubMed:20044574, ECO:0000269|PubMed:20851901}.

Subcellular location: Bacterial microcompartment {ECO:0000305|PubMed:19451619, ECO:0000305|PubMed:20044574, ECO:0000305|PubMed:20851901}.

Domain: Has 2 BMC domains which can evolve independently of each other. {ECO:0000305|PubMed:19451619}.

Similarity: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE- ProRule:PRU01279}.

Annotations taken from UniProtKB at the EBI.


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



Function:		A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation (Probable). Two crystal forms have been seen; a form with a closed central pore that has 3 very small (1.1-2.2 Angstroms) channels per trimer lined by acidic and aromatic residues (PubMed:19451619, PubMed:20044574). A form with a large central pore (8-12 Angstroms) has also been seen; this is probably a functional pore which allows molecules to enter and exit the BMC in a selective, gated manner (PubMed:20851901, PubMed:20044574). Another group only sees the central pore in the presence of Zn(2+); soaking crystals in ZnCl(2) leads to dramatic conformational changes that open a central pore of about 12 Angstroms. Whether Zn(2+) binding is physiologically relevant is unclear, however it suggests a gating mechanism exists (PubMed:20851901). Ethanolamine-binding by the small channels has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (By similarity). {ECO:0000250\|UniProtKB:Q8XLZ0, ECO:0000269\|PubMed:19451619, ECO:0000269\|PubMed:20044574, ECO:0000269\|PubMed:20851901, ECO:0000305\|PubMed:19451619, ECO:0000305\|PubMed:20044574, ECO:0000305\|PubMed:20851901, ECO:0007744\|PDB:3GFH, ECO:0007744\|PDB:3I82, ECO:0007744\|PDB:3MPV}.


Pathway:		Amine and polyamine degradation; ethanolamine degradation.
Subunit:		Homotrimerizes to form a pseudohexamer (PubMed:19194002, PubMed:19451619, PubMed:20851901, PubMed:20044574). The trimers form a two-dimensional array about 37 Angstroms thick (PubMed:19451619, PubMed:20044574). {ECO:0000269\|PubMed:19194002, ECO:0000269\|PubMed:19451619, ECO:0000269\|PubMed:20044574, ECO:0000269\|PubMed:20851901}.
Subcellular location:		Bacterial microcompartment {ECO:0000305\|PubMed:19451619, ECO:0000305\|PubMed:20044574, ECO:0000305\|PubMed:20851901}.
Domain:		Has 2 BMC domains which can evolve independently of each other. {ECO:0000305\|PubMed:19451619}.
Similarity:		Belongs to the EutL/PduB family. {ECO:0000255\|PROSITE- ProRule:PRU01279}.