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.
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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.
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from curated databases
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experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
sltYPutative soluble lytic murein transglycosylase. Homology to slt of E. coli of 24% (sprot|SLT_ECOLI). Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division. InterPro: SLT domain (IPR000189) Pfam: Transglycosylase SLT domain singal peptide no TMHs; High confidence in function and specificity. (642 aa)    
Predicted Functional Partners:
azo0495
Putative NADH dehydrogenase; 33%; Specificity unclear.
       0.771
azo0497
Unnamed protein product; 5-formyltetrahydrofolate cyclo-ligase InterPro: 5-formyltetrahydrofolate cyclo-ligase; Specificity unclear; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
       0.614
azo3349
Putative transglycosylase; Similar to phage protein P7. InterPro: SLT domain; Family membership.
  
   
 0.597
azo3188
Soluble lytic murein transglycosylase precursor (EC 3.2.1.-) (Slt70). Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N- acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity). InterPro: SLT domain; Family membership.
  
   
 0.595
sspA1
Putative stringent starvation protein A. Homology to sspA of E. coli of 26% (sprot|SSPA_ECOLI). FORMS AN EQUIMOLAR COMPLEX WITH THE RNA POLYMERASE HOLOENZYME (RNAP) BUT NOT WITH THE CORE ENZYME. IT IS SYNTHESIZED PREDOMINANTLY WHEN CELLS ARE EXPOSED TO AMINO ACID STARVATION AT WHICH TIME IT ACCOUNTS FOR OVER 50% OF THE TOTAL PROTEIN SYNTHESIZED. InterPro: Glutathione S-transferase N terminus (IPR001045) Pfam: Glutathione S-transferase, N-terminal domaine no signal peptide no TMHs; Family membership.
       0.589
cca1
tRNA-nucleotidyltransferase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
       0.569
azo1074
38% identity with Hypothetical protein from Chromobacterium violaceum TrEMBL:Q7NTL0,Genename CV3044 Signal Peptide present TMHMM reporting for transmembrane helices:2 present; Conserved hypothetical protein.
  
     0.533
pbpA
Penicillin-binding protein; Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily.
 
  
 0.487
azo2060
Membrane-bound lytic murein transglycosylase D; Region start changed from 2259236 to 2259431 (-195 bases).
 
   
 0.474
nlpD
Conserved hypothetical lipoprotein. Homology to nlpD of R. gelatinosus of 43% (trembl|Q9JP90) InterPro: Peptidase family M23/M37 (IPR002886); LysM motif (IPR002482) Pfam: LysM domain; Peptidase family m23/M27 signal peptide no TMHs; Conserved hypothetical protein.
  
   
 0.473
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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