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
mltGConserved hypothetical periplasmic protein; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. (347 aa)    
Predicted Functional Partners:
CAZ94079.1
The N-Acetyltransferases catalyze the transfer of an acetyl group from acetyl-CoA to a substrate molecule; Belongs to Gcn5 or GNAT actyltransferase family; Localized in the cytoplasm; Family membership.
       0.820
dapF
Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine.
       0.820
pbp1A
Penicillin-binding protein 1A, family GT51; Penicillin-binding protein 1A is a class A PBP involved in the synthesis of cross-linked peptidoglycan from the lipid II intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). The N-terminal domain belongs to the family 51 of the glycosyltransferases. Features an uncleaved signal peptide. Localized in the periplasm, anchored to the cytoplasmic membrane; High confidence in [...]
 
   
 0.714
pcm
Protein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
      0.691
ftsX
Cell division protein FtsX; Required for cell division and gliding motility. Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.
 
  
 0.589
amiA
N-acetylmuramoyl-L-alanine amidase; The protein contains two domains. A N-terminal N-acetylmuramoyl-L-alanine amidase domain (230 residues) that hydrolyzes the amide bond between N-acetylmuramoyl residues and L-amino acid residues in bacterial cell walls and a C-terminal domain (200 residues) of unknown function; Contains one N-terminal transmembrane segment; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family; Localized in the cytoplasmic membrane; High confidence in function and specificity.
 
   
 0.573
ftsA
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.
 
  
 0.573
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.
 
  
 0.564
degP
Peptidase Do, family S1; Peptidase Do is a heat shock protein which is required for bacterial growth at elevated temperatures. It is involved in the degradation of damaged proteins. Belongs to the family 1 of the serine peptidase. Displays a catalytic triad His, Asp and Ser. Contains a C-terminal PDZ domain. Features an uncleaved signal peptide. Localized in the cytoplasmic membrane; High confidence in function and specificity.
       0.555
pbp1B
Penicillin-binding protein 1B, family GT51; Penicillin-binding protein 1B is a class A PBP involved in the synthesis of cross-linked peptidoglycan from the lipid II intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). The N-terminal domain belongs to the family 51 of the glycosyltransferases. Features an uncleaved signal peptide. Localized in the periplasm, anchored to the cytoplasmic membrane; High confidence in [...]
  
   
 0.552
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
Server load: low (24%) [HD]