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tatB protein (Methylobacter tundripaludum) - STRING interaction network
"tatB" - Sec-independent protein translocase protein TatB in Methylobacter tundripaludum
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
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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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
tatBSec-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)    
Predicted Functional Partners:
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)
 
  0.999
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)
 
  0.997
Mettu_1669
Sec-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)
     
  0.963
Mettu_0055
Bilirubin oxidase (545 aa)
       
 
  0.842
hisE
Phosphoribosyl-ATP pyrophosphatase (105 aa)
              0.795
hisI
Phosphoribosyl-AMP cyclohydrolase ; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP (130 aa)
              0.795
hisF
ImGP 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)
              0.795
hisA
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (244 aa)
              0.795
Mettu_1664
ImGP synthase subunit HisH ; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR (214 aa)
              0.710
hisB
Imidazoleglycerol-phosphate dehydratase (208 aa)
              0.690
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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