| Accession | TIGR01256 |
| Name | modA |
| Function | molybdate ABC transporter, periplasmic molybdate-binding protein |
| Gene Symbol | modA |
| Trusted Cutoff | 62.50 |
| Domain Trusted Cutoff | 62.50 |
| Noise Cutoff | 50.50 |
| Domain Noise Cutoff | 50.50 |
| Isology Type | equivalog |
| HMM Length | 217 |
| Mainrole Category | Transport and binding proteins |
| Subrole Category | Anions |
| Gene Ontology Term | GO:0015412: molybdate transmembrane-transporting ATPase activity molecular_function |
| | GO:0015689: molybdate ion transport biological_process |
| | GO:0030288: outer membrane-bounded periplasmic space cellular_component |
| | GO:0030973: molybdate ion binding molecular_function |
| | GO:0031362: anchored to external side of plasma membrane cellular_component |
| | GO:0055052: ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing cellular_component |
| Author | Ujwal ML, Paulsen IT |
| Entry Date | May 23 2001 11:19AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. |
| Genome Property | GenProp0192: molybdate ABC transporter (HMM) |
