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Mettu_1396 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1396" - Endolytic peptidoglycan transglycosylase RlpA in Methylobacter tundripaludum
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Mettu_1396Endolytic peptidoglycan transglycosylase RlpA; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides (265 aa)    
Predicted Functional Partners:
Mettu_1395
TIGRFAM- Lytic murein transglycosylase B; KEGG- avn-Avin_08410 lytic murein transglycosylase B (340 aa)
   
        0.856
Mettu_1397
Beta-lactamase; KEGG- mca-MCA0105 D-alanyl-D-alanine carboxypeptidase; PFAM- Peptidase S11, D-alanyl-D-alanine carboxypeptidase A; Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal; Belongs to the peptidase S11 family (389 aa)
   
        0.767
Mettu_1399
UPF0250 protein Mettu_1399; KEGG- tbd-Tbd_0268 hypothetical protein; HAMAP- Protein of unknown function DUF493; PFAM- Protein of unknown function DUF493; Belongs to the UPF0250 family (87 aa)
   
        0.742
Mettu_1398
D-amino-acid transaminase; KEGG- mca-MCA0106 D-amino acid aminotransferase, putative; PFAM- Aminotransferase, class IV (280 aa)
              0.740
mrdB
Peptidoglycan glycosyltransferase MrdB; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily (377 aa)
 
   
  0.724
lipB
Octanoyltransferase; 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 (202 aa)
   
        0.682
lipA
Lipoyl synthase; 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 (320 aa)
   
        0.681
mrdA
Peptidoglycan D,D-transpeptidase MrdA; Catalyzes cross-linking of the peptidoglycan cell wall; Belongs to the transpeptidase family. MrdA subfamily (612 aa)
 
   
  0.633
Mettu_1392
Rod shape-determining protein MreD; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins (161 aa)
 
     
  0.577
Mettu_1391
KEGG- mca-MCA0101 rod shape-determining protein MreC; TIGRFAM- Rod shape-determining protein MreC, subtype; PFAM- Rod shape-determining protein MreC (339 aa)
   
        0.502
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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