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DVU_1607 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_1607" - Uncharacterized protein in Desulfovibrio vulgaris Hildenborough
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
DVU_1607Uncharacterized protein; Identified by Glimmer2; putative (248 aa)    
Predicted Functional Partners:
DVU_1606
Potassium uptake protein, TrkA family; Identified by similarity to OMNI-NTL01SS00580; match to protein family HMM PF02080; match to protein family HMM PF02254 (350 aa)
              0.857
uvrB
UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] (677 aa)
              0.857
ligA
DNA ligase; DNA ligase that catalyzes the formation of phosphodiester linkages between 5’-phosphoryl and 3’-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA (799 aa)
              0.742
DVU_1604
Uncharacterized protein; Identified by Glimmer2; putative (192 aa)
              0.640
dapB
4-hydroxy-tetrahydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy- tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family (259 aa)
              0.447
nadE
Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source (559 aa)
              0.422
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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