STRINGSTRING
ompB protein (Chlamydia trachomatis) - STRING interaction network
"ompB" - annotation not available in Chlamydia trachomatis
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.
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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
ompBannotation not available (340 aa)    
Predicted Functional Partners:
pmpD
annotation not available (1530 aa)
           
  0.660
ompA
Major outer membrane porin, serovar F; In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the large cysteine-rich periplasmic protein. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan (By similarity) (395 aa)
           
  0.660
omcB
Large cysteine-rich periplasmic protein OmcB, serovar E; In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the major outer membrane protein. It has been described in publications as the Sarkosyl- insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan (By similarity) (553 aa)
           
  0.660
aaxA
Porin; Facilitates L-arginine uptake, as part of the AaxABC system. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response (466 aa)
           
  0.660
omcA
Small cysteine-rich outer membrane protein OmcA; In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the large cysteine-rich periplasmic protein and the major outer membrane porin. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan (By similarity) (88 aa)
           
  0.639
tarp
annotation not available (1007 aa)
           
  0.596
pbp
annotation not available (647 aa)
           
  0.590
pmpA
annotation not available (975 aa)
           
  0.541
pmpE
annotation not available (964 aa)
           
  0.540
O172_03955
annotation not available (455 aa)
              0.529
Your Current Organism:
Chlamydia trachomatis
NCBI taxonomy Id: 813
Other names: ATCC VR-571B, C. trachomatis, Chlamydia trachomatis, Chlamydozoon trachomatis, DSM 19440, Rickettsia trachomae, Rickettsia trachomatis, strain A/Har-13
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