STRINGSTRING
STRING protein interaction network
Nodes:
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Rvan_3649PFAM: RNA-metabolising metallo-beta-lactamase; KEGG: ara:Arad_1867 metallo-beta-lactamase family protein. (562 aa)    
Predicted Functional Partners:
Rvan_3648
KEGG: pla:Plav_3212 biotin--acetyl-CoA-carboxylase ligase; TIGRFAM: biotin/acetyl-CoA-carboxylase ligase; PFAM: biotin/lipoate A/B protein ligase; biotin protein ligase domain protein.
      0.867
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
 
  
 0.766
Rvan_3650
TIGRFAM: methylmalonyl-CoA epimerase; KEGG: xau:Xaut_4617 methylmalonyl-CoA epimerase; PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase.
       0.724
nuoN
Proton-translocating NADH-quinone oxidoreductase, chain N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family.
  
    0.714
Rvan_3645
TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; KEGG: azc:AZC_1679 NADH-plastoquinone oxidoreductase chain 5 protein; PFAM: NADH/Ubiquinone/plastoquinone (complex I); NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; NADH dehydrogenase subunit 5 domain protein.
  
    0.710
Rvan_3646
KEGG: rpb:RPB_2586 NADH dehydrogenase subunit M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
       0.704
nuoK
NADH-ubiquinone oxidoreductase chain 4L; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family.
       0.701
Rvan_3643
NADH-ubiquinone/plastoquinone oxidoreductase chain 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
       0.700
Rvan_3651
KEGG: apb:SAR116_0159 protein of unknown function DUF1467.
       0.686
tolB
Tol-Pal system beta propeller repeat protein TolB; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
      0.662
Your Current Organism:
Rhodomicrobium vannielii
NCBI taxonomy Id: 648757
Other names: R. vannielii ATCC 17100, Rhodomicrobium vannielii ATCC 17100, Rhodomicrobium vannielii NCIMB 10020, Rhodomicrobium vannielii str. ATCC 17100, Rhodomicrobium vannielii strain ATCC 17100
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