UniProt functional annotation for P54582



	UniProt functional annotation for P54582

UniProt code: P54582.

Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; Corynebacterium.

Function: Involved in response to osmotic stress (PubMed:7642496, PubMed:9446558, PubMed:10625602, PubMed:19262666, PubMed:21364531, PubMed:24141878). High-affinity glycine betaine-specific uptake system, which couples the uptake of glycine betaine to the symport of two Na(+) ions (PubMed:7642496, PubMed:10625602, PubMed:15134432, PubMed:19262666, PubMed:21364531, PubMed:22940865, PubMed:24141878). Transport is driven both by the Na(+) gradient and by the electrical potential (PubMed:7642496, PubMed:10625602). In addition, functions both as an osmosensor and as an osmoregulator that transduces signal to the catalytic part of the carrier protein, which adapts its activity to the extent of osmotic stress (PubMed:9446558, PubMed:10625602, PubMed:11574473). {ECO:0000269|PubMed:10625602, ECO:0000269|PubMed:11574473, ECO:0000269|PubMed:15134432, ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:22940865, ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:7642496, ECO:0000269|PubMed:9446558}.

Activity regulation: Uptake is activated by hyperosmotic stress (PubMed:7642496, PubMed:9446558, PubMed:10625602, PubMed:15134432, PubMed:19262666, PubMed:21364531, PubMed:24141878). Osmoresponsive activation is triggered by a change in the internal K(+) concentration (PubMed:11574473, PubMed:15063732). In addition, shows a pronounced chill stimulation, at temperatures around 10 degrees Celsius (PubMed:15995189, PubMed:17693504). Chill activation may be influenced by the membrane lipid composition (PubMed:17693504). Uptake is completely abolished by the uncoupler CCCP, and to a different extent by the ionophores valinomycin and nigericin (PubMed:7642496). {ECO:0000269|PubMed:10625602, ECO:0000269|PubMed:11574473, ECO:0000269|PubMed:15063732, ECO:0000269|PubMed:15134432, ECO:0000269|PubMed:15995189, ECO:0000269|PubMed:17693504, ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:7642496, ECO:0000269|PubMed:9446558}.

Biophysicochemical properties: Kinetic parameters: KM=8.6 uM for glycine betaine {ECO:0000269|PubMed:7642496}; KM=3.6 uM for glycine betaine {ECO:0000269|PubMed:10625602}; KM=3.5 uM for glycine betaine {ECO:0000269|PubMed:21364531}; KM=3 uM for glycine betaine {ECO:0000269|PubMed:15134432}; KM=4.1 mM for Na(+) {ECO:0000269|PubMed:7642496}; KM=15 mM for Na(+) {ECO:0000269|PubMed:10625602}; KM=38.1 mM for Na(+) {ECO:0000269|PubMed:15134432}; Vmax=110 nmol/min/mg enzyme {ECO:0000269|PubMed:7642496}; Vmax=2.3 mmol/min/mg enzyme {ECO:0000269|PubMed:10625602}; Vmax=2264 nmol/min/mg enzyme {ECO:0000269|PubMed:21364531}; Vmax=1693 nmol/min/mg enzyme {ECO:0000269|PubMed:15134432}; pH dependence: Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:7642496};

Subunit: Homotrimer (PubMed:15046983, PubMed:21681199, PubMed:19262666, PubMed:21364531, PubMed:22940865, PubMed:24141878, PubMed:25023443). The monomer can accumulate glycine betaine, but trimerization is required to properly respond to osmotic stress (PubMed:21681199). {ECO:0000269|PubMed:15046983, ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:21681199, ECO:0000269|PubMed:22940865, ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:25023443}.

Subcellular location: Cell inner membrane {ECO:0000269|PubMed:17390131, ECO:0000269|PubMed:19262666}; Multi-pass membrane protein {ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:22940865, ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:25023443}.

Induction: Constitutively expressed at a basal level of activity (PubMed:7642496). Induced upon hyperosmotic conditions, resulting in an increase of its transport activity (PubMed:7642496, PubMed:17390131). {ECO:0000269|PubMed:17390131, ECO:0000269|PubMed:7642496}.

Domain: Contains a negatively charged N-terminus and a positively charged C-terminus, which are both involved in sensing and/or transducing osmotic changes to the domain responsible for the translocation of the substrate glycine betaine (PubMed:9446558). The C- terminal domain is directly involved in K(+) sensing or K(+)-dependent activation of BetP (PubMed:15134432). {ECO:0000269|PubMed:15134432, ECO:0000269|PubMed:9446558}.

Disruption phenotype: Mutant shows strongly decreased glycine betaine uptake. {ECO:0000269|PubMed:8752342}.

Similarity: Belongs to the BCCT transporter (TC 2.A.15) family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; Corynebacterium.



Function:		Involved in response to osmotic stress (PubMed:7642496, PubMed:9446558, PubMed:10625602, PubMed:19262666, PubMed:21364531, PubMed:24141878). High-affinity glycine betaine-specific uptake system, which couples the uptake of glycine betaine to the symport of two Na(+) ions (PubMed:7642496, PubMed:10625602, PubMed:15134432, PubMed:19262666, PubMed:21364531, PubMed:22940865, PubMed:24141878). Transport is driven both by the Na(+) gradient and by the electrical potential (PubMed:7642496, PubMed:10625602). In addition, functions both as an osmosensor and as an osmoregulator that transduces signal to the catalytic part of the carrier protein, which adapts its activity to the extent of osmotic stress (PubMed:9446558, PubMed:10625602, PubMed:11574473). {ECO:0000269\|PubMed:10625602, ECO:0000269\|PubMed:11574473, ECO:0000269\|PubMed:15134432, ECO:0000269\|PubMed:19262666, ECO:0000269\|PubMed:21364531, ECO:0000269\|PubMed:22940865, ECO:0000269\|PubMed:24141878, ECO:0000269\|PubMed:7642496, ECO:0000269\|PubMed:9446558}.


Activity regulation:		Uptake is activated by hyperosmotic stress (PubMed:7642496, PubMed:9446558, PubMed:10625602, PubMed:15134432, PubMed:19262666, PubMed:21364531, PubMed:24141878). Osmoresponsive activation is triggered by a change in the internal K(+) concentration (PubMed:11574473, PubMed:15063732). In addition, shows a pronounced chill stimulation, at temperatures around 10 degrees Celsius (PubMed:15995189, PubMed:17693504). Chill activation may be influenced by the membrane lipid composition (PubMed:17693504). Uptake is completely abolished by the uncoupler CCCP, and to a different extent by the ionophores valinomycin and nigericin (PubMed:7642496). {ECO:0000269\|PubMed:10625602, ECO:0000269\|PubMed:11574473, ECO:0000269\|PubMed:15063732, ECO:0000269\|PubMed:15134432, ECO:0000269\|PubMed:15995189, ECO:0000269\|PubMed:17693504, ECO:0000269\|PubMed:19262666, ECO:0000269\|PubMed:21364531, ECO:0000269\|PubMed:24141878, ECO:0000269\|PubMed:7642496, ECO:0000269\|PubMed:9446558}.
Biophysicochemical properties:		Kinetic parameters: KM=8.6 uM for glycine betaine {ECO:0000269\|PubMed:7642496}; KM=3.6 uM for glycine betaine {ECO:0000269\|PubMed:10625602}; KM=3.5 uM for glycine betaine {ECO:0000269\|PubMed:21364531}; KM=3 uM for glycine betaine {ECO:0000269\|PubMed:15134432}; KM=4.1 mM for Na(+) {ECO:0000269\|PubMed:7642496}; KM=15 mM for Na(+) {ECO:0000269\|PubMed:10625602}; KM=38.1 mM for Na(+) {ECO:0000269\|PubMed:15134432}; Vmax=110 nmol/min/mg enzyme {ECO:0000269\|PubMed:7642496}; Vmax=2.3 mmol/min/mg enzyme {ECO:0000269\|PubMed:10625602}; Vmax=2264 nmol/min/mg enzyme {ECO:0000269\|PubMed:21364531}; Vmax=1693 nmol/min/mg enzyme {ECO:0000269\|PubMed:15134432}; pH dependence: Optimum pH is 7.5-8.5. {ECO:0000269\|PubMed:7642496};
Subunit:		Homotrimer (PubMed:15046983, PubMed:21681199, PubMed:19262666, PubMed:21364531, PubMed:22940865, PubMed:24141878, PubMed:25023443). The monomer can accumulate glycine betaine, but trimerization is required to properly respond to osmotic stress (PubMed:21681199). {ECO:0000269\|PubMed:15046983, ECO:0000269\|PubMed:19262666, ECO:0000269\|PubMed:21364531, ECO:0000269\|PubMed:21681199, ECO:0000269\|PubMed:22940865, ECO:0000269\|PubMed:24141878, ECO:0000269\|PubMed:25023443}.
Subcellular location:		Cell inner membrane {ECO:0000269\|PubMed:17390131, ECO:0000269\|PubMed:19262666}; Multi-pass membrane protein {ECO:0000269\|PubMed:19262666, ECO:0000269\|PubMed:21364531, ECO:0000269\|PubMed:22940865, ECO:0000269\|PubMed:24141878, ECO:0000269\|PubMed:25023443}.
Induction:		Constitutively expressed at a basal level of activity (PubMed:7642496). Induced upon hyperosmotic conditions, resulting in an increase of its transport activity (PubMed:7642496, PubMed:17390131). {ECO:0000269\|PubMed:17390131, ECO:0000269\|PubMed:7642496}.
Domain:		Contains a negatively charged N-terminus and a positively charged C-terminus, which are both involved in sensing and/or transducing osmotic changes to the domain responsible for the translocation of the substrate glycine betaine (PubMed:9446558). The C- terminal domain is directly involved in K(+) sensing or K(+)-dependent activation of BetP (PubMed:15134432). {ECO:0000269\|PubMed:15134432, ECO:0000269\|PubMed:9446558}.
Disruption phenotype:		Mutant shows strongly decreased glycine betaine uptake. {ECO:0000269\|PubMed:8752342}.
Similarity:		Belongs to the BCCT transporter (TC 2.A.15) family. {ECO:0000305}.