STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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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pupProkaryotic ubiquitin-like protein Pup; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the FabD, PanB and Mpa proteins. Belongs to the prokaryotic ubiquitin-like protein family. (64 aa)    
Predicted Functional Partners:
prcB
Proteasome beta subunit PrcB; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...]
 
 
 0.999
prcA
Proteasome alpha subunit PrcA; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...]
 
 
 0.998
mpa
Mycobacterial proteasome ATPase Mpa; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Is required but not sufficient to confer resistance against the lethal effects of reactiv [...]
 
 
 0.997
dop
Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily.
 
  
 0.967
pafA
Proteasome accessory factor a PafA; Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine. PafA is required to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types.
 
  
 0.926
bpa
Conserved protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family.
  
  
 0.694
sseC1
Rv3118, (MTCY164.28, O05794), len: 100 aa. SseC1,conserved hypothetical protein, equivalent to Q9CBC7|ML2199 hypothetical protein from Mycobacterium leprae (100 aa),FASTA scores: opt: 545, E(): 3.1e-30, (84.0% identity in 10 aa overlap). Also similar to hypothetical proteins e.g. Q50035 from Saccharopolyspora erythraea (Streptomyces erythraeus) (101 aa), FASTA scores: opt: 345, E(): 9.7e-17,(57.15% identity in 98 aa overlap); and Q9K4H3|SCD66.02 from Streptomyces coelicolor (95 aa), FASTA scores: opt: 249, E(): 2.8e-10, (48.5% identity in 99 aa overlap). Some weak similarity with Q9ZB8 [...]
  
  
 0.630
Rv1457c
Rv1457c, (MTV007.04c), len: 261 aa. Possible unidentified antibiotic-transport integral membrane protein ABC transporter (see citation below), equivalent to Z99125|MLCL536.32 from Mycobacterium leprae (265 aa), FASTA scores: opt: 1415, E(): 0, (83.1% identity in 260 aa overlap).
  
     0.463
mshD
GCN5-related N-acetyltransferase, MshD; Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol. Belongs to the acetyltransferase family. MshD subfamily.
  
    0.460
rbpA
Conserved protein; Binds to RNA polymerase (RNAP), stimulating and stabilizing the formation of stable RNAP promoter complexes up to 2-fold from principal sigma factor SigA-dependent but not alternative sigma factor SigF-dependent promoters. Increases the affinity of core RNAP for SigA, increasing the transcriptional activity of RNAP. Unlike the case in M.smegmatis or S.coelicolor, has no effect on rifampicin inhibition of transcription. Has no effect on E.coli RNAP. Belongs to the RNA polymerase-binding protein RbpA family.
   
  
 0.440
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
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