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
mutSDNA mismatch repair protein MutS; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. (878 aa)    
Predicted Functional Partners:
mutL
DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
 
 0.997
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
   
 0.982
AGB40040.1
DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
   
 0.981
AGB42036.1
Flagellar biosynthesis/type III secretory pathway protein; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.
  
 0.968
mutS2
MutS2 family protein; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily.
 
 
0.937
AGB41761.1
single-stranded-DNA-specific exonuclease RecJ; PFAM: DHH family; DHHA1 domain; DEAD/DEAH box helicase; TIGRFAM: single-stranded-DNA-specific exonuclease RecJ.
 
 0.752
topA
DNA topoisomerase I, bacterial; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removi [...]
 
 0.713
miaA
tRNA isopentenyltransferase MiaA; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family.
 
     0.713
AGB40924.1
PFAM: Protein of unknown function (DUF964); Belongs to the UPF0342 family.
       0.652
miaB
tRNA-N(6)-(isopentenyl)adenosine-37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
       0.634
Your Current Organism:
Halobacteroides halobius
NCBI taxonomy Id: 748449
Other names: H. halobius DSM 5150, Halobacteroides halobius ATCC 35273, Halobacteroides halobius DSM 5150, Halobacteroides halobius MD-1, Halobacteroides halobius str. DSM 5150, Halobacteroides halobius strain DSM 5150
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.