STRINGSTRING
ctaB protein (Alcaligenes faecalis) - STRING interaction network
"ctaB" - Protoheme IX farnesyltransferase in Alcaligenes faecalis
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily (297 aa)    
Predicted Functional Partners:
JT27_06505
Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method- Protein Homology (357 aa)
  0.999
JT27_06540
Cytochrome c oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (535 aa)
 
 
  0.986
JT27_06545
Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B) (386 aa)
 
 
  0.985
JT27_06525
MFS transporter; Derived by automated computational analysis using gene prediction method- Protein Homology (291 aa)
 
   
  0.981
JT27_06515
SURF1-like protein; Derived by automated computational analysis using gene prediction method- Protein Homology (260 aa)
 
 
  0.978
JT27_06510
Membrane protein; Derived by automated computational analysis using gene prediction method- Protein Homology (209 aa)
 
   
  0.958
hemH
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family (361 aa)
     
 
  0.953
JT27_06520
Membrane protein; Derived by automated computational analysis using gene prediction method- Protein Homology (68 aa)
 
          0.812
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (905 aa)
   
   
  0.757
JT27_02415
Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method- Protein Homology (205 aa)
   
  0.731
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
Server load: low (9%) [HD]