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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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MPLPutative UDP-N-acetylmuramate-alanine ligase; Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl- meso-diaminopimelate by linking it to UDP-N-acetylmuramate. Belongs to the MurCDEF family. Mpl subfamily. (452 aa)    
Predicted Functional Partners:
murG
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily.
 
  
 0.912
MURD
Putative UDP-N-acetylmuramoylalanine-D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family.
 
  
 0.891
STY0144
Hypothetical UDP-N-acetylmuramoylalanyl-D-glutamyl-2, 6-diaminopimelate--D-alanyl-D-alanyl ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily.
 
  
 0.878
C0111
Hypothetical cell division protein FtsQ; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
  
  
 0.863
CV3337
Putative 3-octaprenyl-4-hydroxybenzoate carboxy-lyase; Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN; Belongs to the UbiX/PAD1 family.
  
  
 0.855
ddl
Hypothetical D-alanine-D-alanine ligase B; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
  
 0.776
STY0147
Putative cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily.
 
  
 0.738
S0084
Putative UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelateligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily.
  
 0.728
ddl-2
Putative D-alanine-D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
  
 0.709
BFL145
Putative cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family.
 
  
 0.696
Your Current Organism:
Photobacterium profundum
NCBI taxonomy Id: 298386
Other names: P. profundum SS9, Photobacterium SS9, Photobacterium profundum SS9, Photobacterium profundum str. SS9, Photobacterium profundum strain SS9, Photobacterium sp. (strain SS9), Photobacterium sp. SS9, deep-sea eubacterium SS9
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.