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
thiEThiamin-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family. (226 aa)    
Predicted Functional Partners:
thiM
Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ); Belongs to the Thz kinase family.
 
 0.999
thiD
Phosphomethylpyrimidine kinase (thiD); Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
 
 0.999
HI_0358
Transcriptional activator, putative; Similar to GB:AE000511 PID:2314455 percent identity: 34.29; identified by sequence similarity; putative; Belongs to the thiaminase-2 family.
 
 0.971
thiL
Thiamin-monophosphate kinase (thiL); Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family.
    
 0.853
moeB
Molybdopterin biosynthesis protein (moeB); Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD; Belongs to the HesA/MoeB/ThiF family.
 
 
 0.781
HI_0418
Transport protein, putative; Similar to GB:L42023 SP:P44610 PID:1003458 PID:1222206 PID:1204537 percent identity: 60.92; identified by sequence similarity; putative.
       0.773
licA
Lic-1 operon protein (licA); Mediates phase variation of the LPS epitopes. Phase variation of H.influenza LPS epitopes expressed by LicA is determined by a translational switch (By similarity).
     
 0.569
rsgA
Conserved hypothetical protein; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit; Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.
     
 0.567
mutT
Mutator mutT protein (mutT); Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate (By similarity); Belongs to the Nudix hydrolase family.
     
 0.488
HI_0419
Protease, putative; Similar to GB:U00096 SP:P76403 PID:1736789 PID:1736801 PID:1788397 percent identity: 79.52; identified by sequence similarity; putative; Belongs to the peptidase U32 family.
  
    0.465
Your Current Organism:
Haemophilus influenzae
NCBI taxonomy Id: 71421
Other names: H. influenzae Rd KW20, Haemophilus influenzae KW20, Haemophilus influenzae Rd, Haemophilus influenzae Rd KW20
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.