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JT27_01690 protein (Alcaligenes faecalis) - STRING interaction network
"JT27_01690" - ABC transporter in Alcaligenes faecalis
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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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[Homology]
Score
JT27_01690ABC transporter; Derived by automated computational analysis using gene prediction method- Protein Homology (635 aa)    
Predicted Functional Partners:
prmB
50S ribosomal protein L3 glutamine methyltransferase; Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue (302 aa)
 
        0.851
dapE
Succinyl-diaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L- diaminopimelic acid (SDAP), forming succinate and LL-2,6- diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily (378 aa)
   
        0.824
dapD
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the transferase hexapeptide repeat family (272 aa)
   
        0.822
rpsG
30S ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA (156 aa)
   
      0.488
ychF
Ribosome-binding ATPase YchF; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner (363 aa)
 
      0.466
rplE
50S ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs (179 aa)
     
      0.449
rplA
50S ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (231 aa)
     
      0.447
msbA
Lipid A export ATP-binding/permease protein MsbA; Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation; Belongs to the ABC transporter superfamily. Lipid exporter (TC 3.A.1.106) family (594 aa)
   
   
  0.418
rpmG
50S ribosomal protein L33; In Escherichia coli BM108, a mutation that results in lack of L33 synthesis had no effect on ribosome synthesis or function; there are paralogous genes in several bacterial genomes, and a CXXC motif for zinc binding and an upstream regulation region of the paralog lacking this motif that are regulated by zinc similar to other ribosomal proteins like L31; the proteins in this group lack the CXXC motif; Derived by automated computational analysis using gene prediction method- Protein Homology (55 aa)
     
      0.417
JT27_13420
Methionine aminopeptidase; Derived by automated computational analysis using gene prediction method- Protein Homology (267 aa)
 
      0.414
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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