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
msrPConserved hypothetical protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R [...] (318 aa)    
Predicted Functional Partners:
msrQ
Conserved hypothetical membrane protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subu [...]
 
  
 0.995
azo2969
Conserved hypothetical secreted protein. Homology to ebA582 of Azoarcus sp. EbN1 of 37% (gnl|keqq|eba:ebA582(KEGG)). No domains predicted. Signal P reporting signal peptide. No TMHs; Conserved hypothetical protein.
   
 0.950
azo2669
Conserved hypothetical cytochrome c family protein. Homology to bra0353 of B. suis of 50% (trembl|Q8FWU2). InterPro: Cytochrome c class I (IPR003088). Pfam: cytochrome c. signal peptide. no TMHS; Function unclear.
   
 0.928
cyt1
Probable cytochrome c-552 precursor. Homology to cyt of N. europaea of 50% (sprot|C552_NITEU). ELECTRON DONOR FOR CYTOCHROME CD1 IN NITRITE AND NITRATE RESPIRATION. InterPro: Cytochrome c class I (IPR003088); Cytochrome c, class ID (IPR002324); cytochrome c, class IC (IPR008168) Pfam: cytochrome c signal peptide no TMHs; High confidence in function and specificity.
   
 0.902
cyt2
Probable cytochrome c-552 precursor. Homology to cyt of N. europaea of 52% (AAB46987). ELECTRON DONOR FOR CYTOCHROME CD1 IN NITRITE AND NITRATE RESPIRATION. InterPro: Cytochrome c class I (IPR003088); cytochrome c,class ID (IPR002324) Pfam: cytochrome c signal peptide no TMHs; High confidence in function and specificity.
   
 0.902
exaA4
Quinoprotein ethanol dehydrogenase precursor (QEDH). Oxidizes primary alcohols and also acts on secondary alcohol, but not highly active on methanol. 37% Bac_PQQ.IPR002372; Bac_PQQ_repeat. Pfam:PF01011; PQQ; 2. Signal peptide:present; High confidence in function and specificity.
   
 0.804
coxB
Conserved hypothetical cytochrome c oxidase,subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 0.790
lapP
Phenol hydroxylase P5 protein (EC 1.14.13.7) (Phenol 2-monooxygenase P5 component). Probable electron transfer from NADPH via FAD and the 2Fe-2S center to the oxygenase activity site of the enzyme; High confidence in function and specificity.
   
 
 0.708
poxF
Probable phenol hydroxylase (EC 1.14.13.7) (Phenol 2-monooxygenase P5 component). Probable electron transfer from NADPH via FAD and the 2Fe-2S center to the oxygenase activity site of the enzyme. InterPro: Oxidoreductase FAD and NAD(P)-binding domain hisT_truA: tRNA pseudouridine synthase A; Specificity unclear.
   
 
 0.708
nagAa
Naphthalene 12-dioxygenase system ferredoxin--NAD(+) reductase component COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. TRANSFERS ELECTRONS FROM FERREDOXIN (NDOA) TO NADH; High confidence in function and specificity.
   
 
 0.708
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.