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
EGW21186.1Cell wall hydrolase/autolysin; KEGG: noc:Noc_0337 N-acetylmuramoyl-L-alanine amidase; PFAM: Cell wall hydrolase/autolysin, catalytic; SMART: Cell wall hydrolase/autolysin, catalytic. (429 aa)    
Predicted Functional Partners:
EGW20058.1
Lytic transglycosylase catalytic; KEGG: cps:CPS_1998 putative membrane-bound lytic murein transglycosylase; PFAM: Lytic transglycosylase-like, catalytic; Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding Lysin subgroup.
 
  
 0.910
EGW21584.1
Rhomboid family protein; PFAM: Peptidase S54, rhomboid; KEGG: mca:MCA1502 rhomboid family protein.
   
   0.878
EGW21173.1
Rhomboid family protein; PFAM: Peptidase S54, rhomboid; KEGG: sta:STHERM_c19270 rhomboid-like protein.
   
   0.878
EGW20165.1
Outer membrane lipoprotein carrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
    
   0.872
lolA
Outer-membrane lipoprotein carrier protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
    
   0.872
EGW22998.1
Sporulation domain-containing protein; PFAM: Sporulation/cell division region, bacteria; KEGG: tgr:Tgr7_0262 hypothetical protein.
 
 0.857
EGW19783.1
Sporulation domain-containing protein; PFAM: Sporulation/cell division region, bacteria; KEGG: tva:TVAG_473590 cell-surface adhesin.
  
 0.789
nnrE
YjeF-related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epi [...]
 
   
 0.740
EGW21185.1
KEGG: mca:MCA1300 hypothetical protein; TIGRFAM: Uncharacterised protein family UPF0079, ATPase bacteria; PFAM: Uncharacterised protein family UPF0079, ATPase bacteria.
  
 
 0.732
mutL
DNA mismatch repair protein mutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
 
   
 0.709
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
Server load: low (16%) [HD]