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
Your Input:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
clpP-2ATP-dependent clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (195 aa)    
Predicted Functional Partners:
clpX
ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
 
 0.996
clpC
Negative regulator of genetic competence ClpC/MecB; PMID: 8016066 best DB hits: BLAST: pir:T36384; probable ATP-binding proteinase - Streptomyces; E=0.0 swissprot:P37571; CLPC_BACSU NEGATIVE REGULATOR OF GENETIC; E=0.0 ddbj:BAB03822.1; (AP001507) class III stress response-related; E=0.0 COG: BS_clpC; COG0542 ATPases with chaperone activity, ATP-binding domain; E=0.0 PFAM: PF02861; Clp amino terminal domain; E=7.5e-19 PF00004; ATPase family associated with; E=1.6e-12 PF02151; UvrB/uvrC motif; E=2.3e-09; Belongs to the ClpA/ClpB family.
 
 
 0.921
clpB
ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.
  
 
 0.907
clpP
ATP-dependent clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
 
  
 
0.842
def
Peptide 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.
 
  
 0.697
grpE
Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...]
   
 
 0.675
dnaK
Chaperone protein HscC; PMID: 9735342 best DB hits: BLAST: swissprot:P77319; HSCC_ECOLI CHAPERONE PROTEIN HSCC (HSC62); E=1e-92 gb:AAG54984.1; AE005244_2 (AE005244) putative dnaK protein; E=3e-91 embl:CAA06391.1; (AJ005129) dnaK [Thermotoga maritima]; E=3e-88 COG: ybeW; COG0443 Molecular chaperone; E=1e-93 PFAM: PF01869; BadF/BadG/BcrA/BcrD ATPase fa; E=0.37 PF00012; Hsp70 protein; E=9.1e-147.
   
 
 0.673
rsmH
Conserved hypothetical protein-putative methyltransferase; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
    
 
 0.663
spoIIIE
Stage III sporulation protein E; PMID: 3129532 PMID: 2507870 PMID: 8160014 best DB hits: BLAST: swissprot:P21458; SP3E_BACSU STAGE III SPORULATION PROTEIN E; E=1e-108 pir:C69999; DNA translocase stage III sporulation homolog ytpT -; E=1e-106 swissprot:P45264; FTSK_HAEIN CELL DIVISION PROTEIN FTSK HOMOLOG; E=1e-105 COG: BS_spoIIIE; COG1674 DNA segregation ATPase FtsK/SpoIIIE and related; E=1e-109 ftsK; COG1674 DNA segregation ATPase FtsK/SpoIIIE and related proteins; E=6e-97 CT739; COG1674 DNA segregation ATPase FtsK/SpoIIIE and related; E=6e-97 PFAM: PF01580; FtsK/SpoIIIE family; E=9.7e-66.
  
  
 0.631
fliP
Flagellar biosynthetic protein fliP-putative tr FT ansporter of flagellar proteins; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family.
      
 0.606
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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