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lipL protein (Bacillus cereus) - STRING interaction network
"lipL" - Octanoyl-[GcvH]:protein N-octanoyltransferase in Bacillus cereus
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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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lipLOctanoyl-[GcvH]-protein N-octanoyltransferase; Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes; Belongs to the octanoyltransferase LipL family (281 aa)    
Predicted Functional Partners:
lipM
Octanoyltransferase LipM; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation (278 aa)
 
     
  0.878
gcvH
Glycine cleavage system H protein; Is also involved in protein lipoylation via its role as an octanoyl/lipoyl carrier protein intermediate; Belongs to the GcvH family (127 aa)
   
 
  0.791
DJ87_190
Uncharacterized protein (170 aa)
   
          0.722
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 (298 aa)
   
   
  0.703
lplJ_1
Lipoate--protein ligase; Lipoyltrans- lipoyltransferase and lipoate-ligase family protein (329 aa)
         
  0.700
DJ87_171
annotation not available (265 aa)
   
        0.657
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (348 aa)
   
   
  0.646
est
annotation not available (246 aa)
   
          0.637
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF- independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (413 aa)
   
   
  0.629
DJ87_3495
annotation not available (297 aa)
 
          0.622
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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