UniProt functional annotation for Q57399



	UniProt functional annotation for Q57399

UniProt code: Q57399.

Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.

Function: Part of the ABC transporter complex MolBCA involved in molybdate import (PubMed:22078568, PubMed:24722984). Responsible for energy coupling to the transport system (PubMed:24722984). Functions as a low-affinity molybdate transporter (PubMed:24722984). {ECO:0000269|PubMed:22078568, ECO:0000269|PubMed:24722984}.

Catalytic activity: Reaction=ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate; Xref=Rhea:RHEA:22020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36264, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.5; Evidence={ECO:0000305|PubMed:24722984};

Activity regulation: The MolBCA complex shows a decrease in affinity in the presence of increasing concentrations of substrate and nucleotide. {ECO:0000269|PubMed:23513215}.

Subunit: The complex is composed of two ATP-binding proteins (MolC), two transmembrane proteins (MolB) and a solute-binding protein (MolA). {ECO:0000269|PubMed:17158291, ECO:0000269|PubMed:19254551, ECO:0000269|PubMed:20173761, ECO:0000269|PubMed:23513215, ECO:0000269|PubMed:23709218}.

Subcellular location: Cell inner membrane {ECO:0000269|PubMed:17158291}; Peripheral membrane protein {ECO:0000269|PubMed:17158291}.

Domain: The transition from the outward-facing to the inward-facing conformation is realized through the asymmetric motion of individual subunits of the transporter (PubMed:19254551). Nucleotide binding is coupled to a conformational shift at the periplasmic gate. This shift is akin to unlocking a swinging door: allowing just enough space for molybdate to slip into the cell. The lower cytoplasmic gate, identified as gate I, remains open throughout the MolBC-A mechanism, and cytoplasmic gate II closes in the presence of nucleotide (PubMed:23709218). {ECO:0000269|PubMed:19254551, ECO:0000269|PubMed:23709218}.

Similarity: Belongs to the ABC transporter superfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.



Function:		Part of the ABC transporter complex MolBCA involved in molybdate import (PubMed:22078568, PubMed:24722984). Responsible for energy coupling to the transport system (PubMed:24722984). Functions as a low-affinity molybdate transporter (PubMed:24722984). {ECO:0000269\|PubMed:22078568, ECO:0000269\|PubMed:24722984}.


Catalytic activity:		Reaction=ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate; Xref=Rhea:RHEA:22020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36264, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.5; Evidence={ECO:0000305\|PubMed:24722984};
Activity regulation:		The MolBCA complex shows a decrease in affinity in the presence of increasing concentrations of substrate and nucleotide. {ECO:0000269\|PubMed:23513215}.
Subunit:		The complex is composed of two ATP-binding proteins (MolC), two transmembrane proteins (MolB) and a solute-binding protein (MolA). {ECO:0000269\|PubMed:17158291, ECO:0000269\|PubMed:19254551, ECO:0000269\|PubMed:20173761, ECO:0000269\|PubMed:23513215, ECO:0000269\|PubMed:23709218}.
Subcellular location:		Cell inner membrane {ECO:0000269\|PubMed:17158291}; Peripheral membrane protein {ECO:0000269\|PubMed:17158291}.
Domain:		The transition from the outward-facing to the inward-facing conformation is realized through the asymmetric motion of individual subunits of the transporter (PubMed:19254551). Nucleotide binding is coupled to a conformational shift at the periplasmic gate. This shift is akin to unlocking a swinging door: allowing just enough space for molybdate to slip into the cell. The lower cytoplasmic gate, identified as gate I, remains open throughout the MolBC-A mechanism, and cytoplasmic gate II closes in the presence of nucleotide (PubMed:23709218). {ECO:0000269\|PubMed:19254551, ECO:0000269\|PubMed:23709218}.
Similarity:		Belongs to the ABC transporter superfamily. {ECO:0000305}.