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RB2654_02189 protein (Maritimibacter alkaliphilus) - STRING interaction network
"RB2654_02189" - LysM domain protein in Maritimibacter alkaliphilus
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second shell of interactors
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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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Score
RB2654_02189LysM domain protein (624 aa)    
Predicted Functional Partners:
RB2654_02184
Cytokinin riboside 5’-monophosphate phosphoribohydrolase (163 aa)
 
          0.781
RB2654_02194
ABC transporter, ATP-binding/permease protein (614 aa)
              0.769
RB2654_11538
LysM domain protein (284 aa)
 
          0.768
topA
DNA topoisomerase I ; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] (846 aa)
              0.640
RB2654_06524
DNA processing protein DprA, putative (375 aa)
   
   
  0.515
cmk
Cytidine monophosphate kinase (203 aa)
   
   
    0.437
RB2654_12164
Ribosomal RNA small subunit methyltransferase B, putative (420 aa)
              0.435
fmt
Methionyl-tRNA formyltransferase ; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP (299 aa)
              0.435
RB2654_11553
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (158 aa)
              0.435
RB2654_11548
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (173 aa)
              0.435
Your Current Organism:
Maritimibacter alkaliphilus
NCBI taxonomy Id: 314271
Other names: M. alkaliphilus, M. alkaliphilus HTCC2654, Maritimibacter, Maritimibacter Lee et al. 2007, Maritimibacter alkaliphilus, Maritimibacter alkaliphilus HTCC2654, Maritimibacter alkaliphilus Lee et al. 2007, Maritimibacter alkaliphilus str. HTCC2654, Maritimibacter alkaliphilus strain HTCC2654, Rhodobacterales bacterium HTCC2654
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