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.
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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:
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
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CAZ97130.1The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator; Family membership. (241 aa)    
Predicted Functional Partners:
CAZ97129.1
The histidine-containing phosphotransfer (HPt) domain is a protein module that mediates phosphotransfer reactions in the two-component signaling systems; HPt modules (~120 residues) contain a histidine residue capable of participating in phosphoryl transfer reactions. They serve as a phosphoreceiver and phosphodonor in order to shuttle phosphoryl groups between two or more response regulator domains; Family membership.
 
     0.883
CAZ97125.1
The HNOB (Heme NO Binding) module, is a predominantly alpha-helical module and binds heme via a covalent linkage to histidine. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals; Probably, acts as effector domain belonging to a two-component system; Family membership.
 
     0.834
CAZ97126.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains three N-terminal PAS/PAC domains involved in many signalling proteins where they are used as a signal sensor domain; Seems localized in the cytoplasm; Family membership.
 
     0.827
CAZ96697.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains four N-terminal transmembrane segments; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.822
CAZ96706.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains four N-terminal transmembrane segments; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.822
CAZ98413.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains four N-terminal transmembrane segments; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.819
CAZ94630.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Signal peptide cleaved between the residues 22 and 23; Contains seven tetratrico peptide repeats (TPR) and one transmembrane segment; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.816
CAZ97383.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains four N-terminal transmembrane segments; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.815
CAZ94193.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains four and two transmembrane segments in the N- and C- terminal domain respectively; Localized in the cytoplasmic membrane; Family membership.
 
 
 0.814
CAZ97128.1
The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Possibly localized in the cytoplasm; Family membership.
 
     0.802
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
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