STRING allows inspection of the interaction evidence for any given network. Choose any of the viewers above (disabled if not applicable in your network).
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
from curated databases
Radical SAM protein, TIGR01212 family; Identified by match to protein family HMM PF04055; match to protein family HMM TIGR01212 (351 aa)
Predicted Functional Partners:
Methylated-DNA--protein-cysteine methyltransferase, DNA-binding domain protein; Identified by match to protein family HMM PF01035; match to protein family HMM TIGR00589 (161 aa)
Rod shape-determining protein MreB; Identified by similarity to SP-P13519; match to protein family HMM TIGR00904 (346 aa)
Cell shape-determining protein MreC; Involved in formation and maintenance of cell shape (304 aa)
Penicillin-binding protein; Identified by similarity to SP-P08150; match to protein family HMM PF00905; match to protein family HMM PF03717 (595 aa)
Uncharacterized protein; Identified by Glimmer2; putative (156 aa)
Peptidoglycan glycosyltransferase MrdB; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily (371 aa)
annotation not available (110 aa)
Uncharacterized protein; Identified by similarity to OMNI-NTL01TT0780; match to protein family HMM PF04519 (115 aa)
Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family (574 aa)
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