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
smtBPutative transcriptional repressor,; High confidence in function and specificity. (103 aa)    
Predicted Functional Partners:
aas
AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...]
     
 0.662
uxuA
Putative mannonate dehydratase; tremblnew|AAR36422:35% identity, 46% similarity EMBL:AE017218; AAR36422.1; TIGR:GSU3030; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in Escherichia coli. Mannonate dehydratase converts D-mannonate to 2-dehydro-3-deoxy-D-gluconate. An apparent equivalog is found in a glucuronate utilization operon in Bacillus stearothermophilus T-6. Interpro:IPR004628;Man_dehyd SignalP predicted signal peptide present. No. of transmembrane helices: 1 (TMHMM predicted) pyrC_dimer: dihydroorotase homodimeric; Specificity unclear.
       0.620
azo0148
Putative acyltransferase family protein; Similar to the Aas bifunctional protein [includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-gpe acyltransferase); acyl-acyl carrier protein synthetase (acyl-acp synthetase)].Plays a role in lysophospholipid acylation. 25% Acyltransferase.IPR000873; AMP-bind. Pfam:PF01553; Acyltransferase; 1.PF00501; AMP-binding; 1. TMhelix:10; Function unclear.
     
 0.610
azo0147
Conserved hypothetical membrane protein. Homology to RS05051 of Ralstonia solanacearum of 45% (trembl|Q8Y1A4(SRS)). TMHMM2 reporting the presence of 26 TMH's. Signal P reporting Signal Peptide present. Coils2 program reporting presence of Coiled coil; Conserved hypothetical protein.
       0.550
atpB
Probable ATP synthase A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
       0.510
azo0152
Conserved hypothetical membrane protein. Homology to BB4612 of Bordetella bronchiseptica of 37% (trembl|Q7WEM2(SRS)). No domains predicted. signal peptide 3 TMHs; Conserved hypothetical protein.
       0.509
atpH
Putative ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
 
     0.452
atpE
Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
       0.408
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
Server load: low (22%) [HD]