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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
dacCProbable D-alanyl-D-alanine carboxypeptidase. Homology to dacD of E. coli of 41% (sprot|DACD_ECOLI) Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Pfam: D-alanyl-D-alanine carboxypeptidase signal peptide no TMHs; High confidence in function and specificity; Belongs to the peptidase S11 family. (376 aa)    
Predicted Functional Partners:
mrcA
Probable penicillin-binding protein 1A (PBP-1a) (PBP1a) [Includes: Penicillin- insensitive transglycosylase (EC 2.4.2.-) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.-.-) (DD-transpeptidase)]. Homology to mrcA of N. meningitides of 47% (sprot|PBPA_NEIMA(SRS)) Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (By sim [...]
     
 0.938
dacB
Serine-type D-Ala-D-Ala carboxypeptidase; Penicillin-binding protein 4 precursor (PBP-4) [Includes: D-alanyl-D- alanine carboxypeptidase (EC 3.4.16.4) (DD-peptidase) (DD- carboxypeptidase); D-alanyl-D-alanine-endopeptidase (DD-endopeptidase)]. Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction. PBP4: D-alanyl-D-alanine carboxypeptid; High confidence in function and specificity.
     
 0.908
azo1687
Putative exported protein; Similar to membrane carboxypeptidases; Family membership.
    
 0.775
pbpA
Penicillin-binding protein; Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily.
 
 
 0.771
lipB
LipB protein; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
       0.733
FtsI
Probable peptidoglycan glycosyltransferase; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum; Belongs to the transpeptidase family. FtsI subfamily.
  
 
 0.723
azo0182
Conserved hypothetical protein. Homology to RSC0326 of Ralstonia solanacearum of 53% (tremble:Q8Y2K9) Has PF04359;Protein of unknown function (DUF493);This family includes several proteins of uncharacterised function. InterPro;IPR007454 No Signal Peptdie or TMH present; Belongs to the UPF0250 family.
  
    0.719
daaA
D-alanine aminotransferase (EC 2.6.1.21) (D-aspartate aminotransferase) (D-amino acid aminotransferase) (D-amino acid transaminase) (DAAT). Acts on the D-isomers of alanine Leucine aspartate glutamate aminobutyrate norvaline and asparagine (By similarity). InterPro: Aminotransferases class-IV; High confidence in function and specificity.
       0.701
rodA
Rod shape-determining protein; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily.
 
   
 0.677
lipA
Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
       0.671
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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