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
mepMMurein DD-endopeptidase, space-maker hydrolase, septation protein; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant. (440 aa)    
Predicted Functional Partners:
znuA
Zinc ABC transporter periplasmic binding protein; Involved in the high-affinity zinc uptake transport system.
  
 0.988
mepH
Murein DD-endopeptidase, space-maker hydrolase; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant.
  
  
 0.910
mepS
Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds. Partially suppresses a prc disruption mutant. Belongs to the peptidase C40 family.
  
  
 0.903
amiB
N-acetylmuramoyl-l-alanine amidase II; Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors.
 
   
 0.823
pbpG
D-alanyl-D-alanine endopeptidase; Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD- diaminopimelate-alanine bonds in high-molecular-mass murein sacculi; Belongs to the peptidase S11 family.
  
  
 0.805
lepB
Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family.
 
  
 0.795
nlpI
Lipoprotein involved in osmotic sensitivity and filamentation; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).
   
  
 0.790
slt
Lytic murein transglycosylase, soluble; 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.
 
   
 0.775
lpxM
Myristoyl-acyl carrier protein (ACP)-dependent acyltransferase; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. Can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A. In vitro, can acylate Kdo(2)-lipid IV(A), but acylation of (KDO)2- (lauroyl)-lipid IV(A) is about 100 times faster. In vitro, can use lauroyl-ACP but displays a slight kinetic preference for myristoyl-ACP.
 
    0.770
htpX
Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family.
 
 
  
 0.769
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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