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clpS protein (Methylobacter tundripaludum) - STRING interaction network
"clpS" - ATP-dependent Clp protease adapter protein ClpS in Methylobacter tundripaludum
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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clpSATP-dependent Clp protease adapter protein ClpS; Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (107 aa)    
Predicted Functional Partners:
Mettu_0640
TIGRFAM- ATP-dependent Clp protease ATP-binding subunit clpA; PFAM- ATPase associated with various cellular activities, AAA-2; ATPase, AAA-type, core; Clp, N-terminal; Clp ATPase, C-terminal; KEGG- mca-MCA1789 ATP-dependent Clp protease, ATP-binding subunit ClpA; SMART- ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family (757 aa)
 
  0.998
aat
Leucyl/phenylalanyl-tRNA--protein transferase; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine (231 aa)
 
     
  0.857
clpB
Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family (858 aa)
 
 
  0.809
mnmA
tRNA-specific 2-thiouridylase MnmA; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34 (363 aa)
              0.668
nudJ
Phosphatase NudJ; PFAM- NUDIX hydrolase domain; KEGG- app-CAP2UW1_2937 NUDIX hydrolase; Belongs to the Nudix hydrolase family. NudJ subfamily (153 aa)
              0.668
Mettu_0707
KEGG- mca-MCA0809 acetylornithine aminotransferase, putative; PFAM- Aminotransferase class-III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family (461 aa)
       
 
  0.665
Mettu_2439
HemY domain protein; PFAM- HemY, N-terminal; KEGG- mca-MCA3062 HemY protein, putative (410 aa)
     
      0.656
lipA
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (320 aa)
     
      0.649
ubiE
Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2- polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) (248 aa)
       
      0.644
Mettu_1391
KEGG- mca-MCA0101 rod shape-determining protein MreC; TIGRFAM- Rod shape-determining protein MreC, subtype; PFAM- Rod shape-determining protein MreC (339 aa)
       
      0.644
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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