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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
mtgAMonofunctional biosynthetic peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. (243 aa)    
Predicted Functional Partners:
ADO46766.1
ThiJ/PfpI domain-containing protein; Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate; Belongs to the peptidase C56 family.
       0.805
mrdA
Penicillin-binding protein 2; Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily.
 
 
 
 0.669
mrdA-2
Penicillin-binding protein 2; Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily.
 
 
 
 0.655
mrdB
Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily.
  
 
 
 0.654
ftsN
Cell division protein FtsN; Essential cell division protein that activates septal peptidoglycan synthesis and constriction of the cell. Acts on both sides of the membrane, via interaction with FtsA in the cytoplasm and interaction with the FtsQBL complex in the periplasm. These interactions may induce a conformational switch in both FtsA and FtsQBL, leading to septal peptidoglycan synthesis by FtsI and associated synthases.
   
 
 0.649
ADO46791.1
TIGRFAM: D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase; KEGG: ssn:SSON_3330 D-alanyl-D-alanine carboxypeptidase/endopeptidase; PFAM: peptidase S13 D-Ala-D-Ala carboxypeptidase C.
  
  
 0.632
ADO46765.1
Multi-sensor hybrid histidine kinase; TIGRFAM: PAS sensor protein; PFAM: ATP-binding region ATPase domain protein; PAS fold domain protein; histidine kinase A domain protein; response regulator receiver; Hpt domain protein; KEGG: enc:ECL_04591 aerobic respiration control sensor protein ArcB; SMART: ATP-binding region ATPase domain protein; histidine kinase A domain protein; PAS domain containing protein; response regulator receiver; Hpt domain protein.
     
 0.574
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
  
   
 0.553
ADO47941.1
Beta-lactamase; KEGG: enc:ECL_03334 D-alanyl-D-alanine carboxypeptidase; PFAM: peptidase S11 D-alanyl-D-alanine carboxypeptidase 1; Penicillin-binding protein 5 domain protein; Belongs to the peptidase S11 family.
   
 
 0.551
ADO49223.1
Beta-lactamase; KEGG: kpn:KPN_00871 D-alanyl-D-alanine carboxypeptidase fraction C; PFAM: peptidase S11 D-alanyl-D-alanine carboxypeptidase 1; Penicillin-binding protein 5 domain protein; Belongs to the peptidase S11 family.
   
 
 0.551
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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