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
azo2479Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein. (235 aa)    
Predicted Functional Partners:
cheD
Conserved hypothetical chemotaxis protein CheD; Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis; Belongs to the CheD family.
 
 0.993
fliM
Flagellar motor switch protein fliM. FLIM IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity.
  
 0.991
fliN
Flagellar motor switch protein fliN (Flagellar motor switch protein mopA) (Fragment). FliN is one of three proteins (FliG FliN FliM) that form a switch complex that is proposed to be located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins in addition to contacting components of the motor that determine the dirction of flagellar rotation (by similarity). InterPro: Surface presentation of antigens (SPOA) protein, Flagellar motor switch FliN protein Pfam: Surface presentation of antigens (SPOA) protein no signal peptide no TMHs; High confid [...]
  
 0.984
fliG
Flagellar motor switch protein fliG. FLIG IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION (BY SIMILARITY). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity.
  
 0.979
flgK
Flagellar hook-filament junction protein 1 (HAP1). no signal peptide no TMHs; High confidence in function and specificity.
  
 
 0.957
cheV2
Probable chemotaxis protein, CheW. IPR001789; Response_reg. Pfam: PF01584; CheW. PF00072; Response_reg. SMART: SM00260; CheW. SM00448; REC. Chemotaxis protein cheV. CHEMOTAXIS INVOLVES BOTH A PHOSPHORYLATION-DEPENDENT EXCITATION AND A METHYLATION-DEPENDENT ADAPTATION. CHEV AND CHEW FUNCTION TOGETHER TO COUPLE CHEA ACTIVATION TO METHYL-ACCEPTING CHEMOTAXIS PROTEIN RECEPTOR STATUS AND POSSIBLE CHEA-DEPENDENT PHOSPHORYLATION OF CHEV CONTRIBUTES TO ADAPTATION; High confidence in function and specificity.
  
 
 0.952
azo1817
Conserved hypothetical two-component hybrid sensor and regulator. Homology to ebA6890 of Azoarcus sp. EbN1 of 56% (gnl|keqq|eba:ebA6890(KEGG)). InterPro: IPR003594 ATPbind_ATPase. IPR004358 Bact_sens_pr_C. IPR005467 His_kinase. IPR003661 His_kinA_N. IPR009082 His_kin_homodim. IPR001610 PAC. IPR000700 PAS-assoc_C. IPR000014 PAS_domain. IPR001789 Response_reg. Pfam: PF02518 HATPase_c. PF00512 HisKA. PF00785 PAC. PF00989 PAS. PF00072 Response_reg. SMART: SM00387 HATPase_c. SM00388 HisKA. SM00086 PAC. SM00091 PAS. SM00448 REC. TIGRFAM: TIGR00229 sensory_box; 3 TMHMM reporting 7 transmembra [...]
  
 
 0.926
azo3381
Hypothetical signaling protein.
  
 
 0.907
pilL
Putative pilus biogenese protein, ATPbind_ATPase. IPR004358; Bact_sens_pr_C. IPR002545; CheW. IPR004105; H-kinase_dim. IPR005467; His_kinase. IPR008207; Hpt. IPR008208; Hpt_N. IPR001789; Response_reg. Pfam: PF01584; CheW. PF02895; H-kinase_dim. PF02518; HATPase_c. PF01627; Hpt. PF00072; Response_reg. SMART: SM00260; CheW. SM00387; HATPase_c. SM00073; HPT. SM00448; REC. HTH reporting nucleic acid binding motif; Function unclear.
  
 0.905
flgC
Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.
  
 
 0.894
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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