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UniProt functional annotation for P23847 | ||
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| UniProt code: P23847. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Part of the ABC transporter DppABCDF involved in dipeptide transport (PubMed:1702779, PubMed:7536291, PubMed:10537211). Binds dipeptides and accepts a wide range of side chains, including small neutral, bulky hydrophobic, and positively and negatively charged groups (PubMed:10537211). Tripeptides are poor substrates (PubMed:10537211). DppA alone controls the specificity of the Dpp transporter (PubMed:10537211). In addition, plays a role in chemotaxis toward peptides via interaction with the chemotaxis protein Tap (PubMed:3520334, PubMed:8563629). {ECO:0000269|PubMed:10537211, ECO:0000269|PubMed:1702779, ECO:0000269|PubMed:3520334, ECO:0000269|PubMed:7536291, ECO:0000269|PubMed:8563629}. |
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| Function: | |
Binds heme. When a foreign outer membrane heme receptor is expressed in E.coli, DppABCDF can also transport heme and its precursor, 5-aminolevulinic acid (ALA), from the periplasm into the cytoplasm. {ECO:0000269|PubMed:16905647, ECO:0000269|PubMed:8444807}. |
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| Activity regulation: | |
Heme binding is inhibited by dipeptide. {ECO:0000269|PubMed:16905647}. |
| Subunit: | |
The complex is composed of two ATP-binding proteins (DppD and DppF), two transmembrane proteins (DppB and DppC) and a solute-binding protein (DppA). {ECO:0000269|PubMed:7536291}. |
| Subcellular location: | |
Periplasm {ECO:0000269|PubMed:1702779}. |
| Induction: | |
Expression is repressed by the presence of casamino acids. {ECO:0000269|PubMed:1702779}. |
| Domain: | |
Consists of two distinct domains (I and II) connected by two strands that presumably function as a hinge (PubMed:8527431, PubMed:8563629). Undergoes conformational change upon substrate binding (PubMed:10537211). {ECO:0000269|PubMed:10537211, ECO:0000269|PubMed:8527431, ECO:0000269|PubMed:8563629}. |
| Disruption phenotype: | |
Inactivation of the gene results in the inability of a proline auxotroph to utilize Pro-Gly as a proline source (PubMed:1702779). Inactivation of the gene has no effect on iron-heme utilization, but the double mppA dppA mutant is unable to use heme as iron source (PubMed:16905647). {ECO:0000269|PubMed:16905647, ECO:0000269|PubMed:1702779}. |
| Similarity: | |
Belongs to the bacterial solute-binding protein 5 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.