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
AMM92702.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (71 aa)    
Predicted Functional Partners:
recU
Holliday junction resolvase; Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation; Belongs to the RecU family.
  
     0.757
ypsB
Cell division protein DivIVA; Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation.
  
     0.750
ezrA
Septation ring formation regulator EzrA; Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization; Belongs to the EzrA family.
  
     0.747
spxA_1
ArsR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ArsC family.
  
     0.729
def-2
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
  
    0.729
dnaB
Replication initiation and membrane attachment protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.720
AMM91516.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.714
AMM91810.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0374 family.
 
    0.706
nrnA_2
Oligoribonuclease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.703
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
  
    0.697
Your Current Organism:
Bacillus simplex
NCBI taxonomy Id: 1478
Other names: ATCC 49097, Arthrobacter sp. CHR2P1B2-M, B. simplex, Bacillus maroccanus, Bacillus sp. JP44SK12, Bacillus sp. JP44SK13, Bacillus sp. JP44SK25, Bacillus sp. JP44SK26, Bacillus sp. JP44SK29, Bacillus sp. JP44SK30, Bacillus sp. JP44SK31, Bacillus sp. JP44SK32, CCUG 28889, CIP 106934, IFO 15720, JCM 12307, LMG 11160, LMG:11160, NBRC 15720, NRRL NRS-960
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