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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
asp1Accessory secretory protein Asp1; Derived by automated computational analysis using gene prediction method: Protein Homology. (518 aa)    
Predicted Functional Partners:
asp2
Accessory secretory protein Asp2; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 
 0.996
asp3
Accessory secretory protein Asp3; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 
 0.996
gtfB
Accessory Sec system glycosyltransferase GtfB; Required for polymorphic O-glycosylation of the serine-rich repeat protein in this bacteria. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins usually encoded upstream in the same operon. The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to the substrate protein, attaching the first sugar residue. Stabilizes the glycosylation activity of GtfA. Has no N-acetylglucosaminyl transferase activity on its own.
 
 
 
 0.981
gtfA
Accessory Sec system glycosylation protein GtfA; Required for polymorphic O-glycosylation of the serine-rich repeat protein in this bacteria. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in the substrate protein. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins usually encoded upstream in the same operon.
 
   
 0.965
secY-2
Accessory Sec system translocase SecY2; Part of the accessory SecA2/SecY2 system specifically required for export of possible cell wall proteins. The central subunit of a protein translocation channel.
 
   
 0.921
secA-2
Accessory Sec system translocase SecA2; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
 
 
 
 0.907
AJC95031.1
Cell-wall-anchored protein.
 
     0.580
AJC94929.1
Surface protein.
  
     0.512
AJC95234.1
Capsular biosynthesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.470
dltC
D-alanine--poly(phosphoribitol) ligase subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
  
     0.416
Your Current Organism:
Staphylococcus hyicus
NCBI taxonomy Id: 1284
Other names: ATCC 11249, CCM 2368, CCUG 6509, CIP 81.58, DSM 20459, JCM 2423, LMG 13352, LMG:13352, Micrococcus hyicus, NCTC 10350, S. hyicus, Staphylococcus hyicus hyicus, Staphylococcus hyicus subsp. hyicus
Server load: medium (46%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.