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
nlpDPeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (319 aa)    
Predicted Functional Partners:
appR
RNA polymerase sigma factor RpoS; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response.
  
  
 0.855
amiB
N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.842
surE
Stationary phase survival protein SurE; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.
 
  
 0.816
pcm
protein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
     
 0.791
lepB
Signal peptidase I; Catalyzes the cleavage of the amino-terminal leader peptide from secretory proteins; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family.
 
  
 0.701
mltD
Lytic murein transglycosylase; Catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues; may play a role in recycling muropeptides during cell division and/or cell elongation; in Helicobacter pylori MltD is a endolytic transglycosylase involved mainly in the rearrangement of the peptidoglycan layer of the bacterial cell wall; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.588
amiC
N-acetylmuramoyl-L-alanine amidase; Hydrolyzes the bond between N-acetylmuramic acid and amino acid residues in peptidoglycan; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.564
rlpA
Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
 
 
 0.545
ftsB
Cell division protein FtsB; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
 
     0.541
rlpB
LPS biosynthesis protein; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
  
   
 0.527
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.