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Mettu_1669 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1669" - Sec-independent protein translocase protein TatA 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
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some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Mettu_1669Sec-independent protein translocase protein TatA; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system (70 aa)    
Predicted Functional Partners:
tatB
Sec-independent protein translocase protein TatB; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation (127 aa)
 
  0.992
Mettu_1671
Sec-independent protein translocase protein TatC; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides (270 aa)
 
  0.989
Mettu_2268
TIGRFAM- Twin-arginine translocation protein TatB; KEGG- alv-Alvin_2527 twin-arginine translocation protein, TatB subunit (101 aa)
 
  0.955
Mettu_2269
Sec-independent protein translocase protein TatC; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides (258 aa)
 
  0.929
Mettu_0171
PFAM- Stringent starvation protein B; KEGG- mca-MCA1958 ClpXP protease specificity-enhancing factor (125 aa)
   
   
  0.694
hisA
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; PFAM- Histidine biosynthesis; TIGRFAM- Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; HAMAP- 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; KEGG- mca-MCA2803 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (244 aa)
         
  0.682
hisI
Phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP (130 aa)
   
        0.674
hisE
TIGRFAM- Phosphoribosyl-ATP pyrophosphohydrolase; HAMAP- Phosphoribosyl-ATP pyrophosphatase; KEGG- mca-MCA2800 phosphoribosyl-ATP pyrophosphatase; PFAM- Phosphoribosyl-ATP pyrophosphohydrolase (105 aa)
              0.670
hisF
Imidazole glycerol phosphate synthase subunit HisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (257 aa)
              0.670
Mettu_0172
PFAM- Glutathione S-transferase, N-terminal; KEGG- mca-MCA1959 stringent starvation protein A (211 aa)
   
   
  0.589
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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