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Mettu_0421 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_0421" - Peptidyl-prolyl cis-trans isomerase 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
Others
textmining
co-expression
protein homology
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Mettu_0421Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (193 aa)    
Predicted Functional Partners:
Mettu_0730
KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype (448 aa)
   
  0.940
lpxH
UDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (241 aa)
 
      0.831
Mettu_4107
Peptidyl-prolyl cis-trans isomerase; Manually curated; KEGG- amc-MADE_03986 putative periplasmic peptidyl-prolyl cis-trans isomerase; PFAM- Peptidyl-prolyl cis-trans isomerase, FKBP-type; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal (160 aa)
 
  0.796
Mettu_1173
KEGG- pna-Pnap_4661 hypothetical protein (363 aa)
     
  0.788
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (642 aa)
   
  0.786
Mettu_4189
TIGRFAM- RNA helicase, ATP-dependent DEAH box, HrpA type; PFAM- Helicase-associated region; DNA/RNA helicase, C-terminal; Domain of unknown function DUF1605; KEGG- mca-MCA1482 ATP-dependent helicase HrpA; SMART- DEAD-like helicase, N-terminal; ATPase, AAA+ type, core; DNA/RNA helicase, C-terminal (1315 aa)
       
  0.773
Mettu_2595
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (694 aa)
   
  0.757
Mettu_1336
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (698 aa)
   
  0.757
Mettu_2137
PFAM- ATP-binding region, ATPase-like; KEGG- rpe-RPE_2484 ATPase domain-containing protein (886 aa)
     
  0.743
Mettu_0271
PFAM- ATP-binding region, ATPase-like; KEGG- rpa-RPA0369 aminoacyl-tRNA synthetase, class I-ATP-binding region, ATPase-like (862 aa)
     
  0.743
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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