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
SFV41106.1ATP-dependent DNA helicase UvrD/PcrA. (742 aa)    
Predicted Functional Partners:
ligA
DNA ligase; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA; Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
 
  
 0.937
SFV40140.1
DNA helicase.
    
 0.914
SFV41230.1
DNA helicase.
    
 0.914
SFV39422.1
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 [...]
 
 
 0.900
recA
RecA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
  
 
 0.886
uvrB
Excinuclease ABC subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...]
 
 
 0.876
SFV41104.1
Putative pheromone cAM373 precursor lipoprotein CamS.
  
  
 0.857
SFV40623.1
ATP-dependent DNA helicase RecQ.
 
 
 0.835
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.
  
 
 0.834
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
 
 
 
 0.825
Your Current Organism:
Lactobacillus acidipiscis
NCBI taxonomy Id: 89059
Other names: CCUG 42961 [[Lactobacillus cypricasei]], CCUG 46556, CIP 106393 [[Lactobacillus cypricasei]], CIP 106750, DSM 15353 [[Lactobacillus cypricasei]], DSM 15836, JCM 10692, KCTC 13900 [[Lactobacillus cypricasei]], L. acidipiscis, Lactobacillus acidipiscis Tanasupawat et al. 2000, Lactobacillus cypricasei, Lactobacillus cypricasei Lawson et al. 2001, Lactobacillus sp. FS60-1, Lactobacillus sp. FS60-1T, Lactobacillus sp. LMG 17676, Lactobacillus sp. LMK3, NBRC 102163, NRIC 0300, PCU 207, PCU:207, strain FS60-1, strain LMK3 [[Lactobacillus cypricasei]]
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