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
sbcCExonuclease (sbcC); SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity (By similarity); Belongs to the SMC family. SbcC subfamily. (1047 aa)    
Predicted Functional Partners:
polA
DNA polymerase I (polA); In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
  
 0.999
sbcD
Exonuclease, putative; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.
 
 0.999
recQ
ATP-dependent DNA helicase, putative; Similar to GB:M87049 SP:P15043 GB:M30198 PID:147559 PID:148221 percent identity: 38.81; identified by sequence similarity; putative.
 
 0.996
topA
DNA topoisomerase I (topA); 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 removing D [...]
  
 0.988
recA
recA protein (recA); 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.
  
 0.967
asnS
asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative.
  
 
  0.869
TP_0939
Pyruvate oxidoreductase; Similar to PID:1001780 SP:P52965 PID:1006618 percent identity: 58.44; identified by sequence similarity; putative.
     
 0.838
TP_0623
Membrane-bound lytic murein transglycosylase D (dniR); Similar to SP:P23931 GB:X60739 PID:1208972 PID:581068 GB:U00096 percent identity: 32.28; identified by sequence similarity; putative.
  
    0.779
TP_0624
Conserved hypothetical protein; Similar to GB:AE000783 percent identity: 21.58; identified by sequence similarity; putative.
       0.773
TP_0625
Predicted coding region TP0625; Hypothetical protein; identified by Glimmer; putative.
       0.773
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.