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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
RB6827Serine/threonine protein kinase; PMID: 9384377 best DB hits: BLAST: pir:H69878; probable protein kinase (EC 2.7.1.-) yloP - Bacillus; E=3e-35 ddbj:BAB06223.1; (AP001515) serinethreonine protein kinase; E=1e-32 embl:CAA10713.1; (AJ132604) hypothetical protein [Lactococcus; E=3e-32 COG: BS_yloP_1; COG0515 Serine/threonine protein kinases; E=2e-36 PFAM: PF00069; Protein kinase domain; E=1.6e-49 PF00480; ROK family; E=0.13. (966 aa)    
Predicted Functional Partners:
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 [...]
  
 
 0.930
Pph1
Probable protein phosphatase 1; PMID: 11298281 best DB hits: BLAST: gb:AAF81068.1; AF223364_3 (AF223364) protein phosphatase 1; E=9e-32 pir:E71538; hypothetical protein CT259 - Chlamydia trachomatis; E=4e-28 pir:H75265; conserved hypothetical protein - Deinococcus radiodurans; E=5e-28 COG: CT259; COG0631 Protein serine/threonine phosphatases; E=4e-29 PFAM: PF00481; Protein phosphatase 2C; E=4.9e-09.
 
 
 0.857
RB3245
Protein phosphatase 1; PMID: 11298281 best DB hits: BLAST: gb:AAF81068.1; AF223364_3 (AF223364) protein phosphatase 1; E=3e-27 pir:E71538; hypothetical protein CT259 - Chlamydia trachomatis; E=5e-26 embl:CAA10712.1; (AJ132604) pppL protein [Lactococcus lactis]; E=2e-25 COG: CT259; COG0631 Protein serine/threonine phosphatases; E=4e-27 PFAM: PF00481; Protein phosphatase 2C; E=1.2e-09.
 
 
 0.856
dnaJ
DnaJ1 protein; PMID: 8016869 PMID: 9276481 best DB hits: BLAST: embl:CAA10745.1; (AJ132708) DnaJ1 protein [Anabaena sp.]; E=1e-39 swissprot:P50027; DNJH_SYNY3 DNAJ-LIKE PROTEIN SLR0093 -----; E=1e-39 embl:CAA10739.1; (AJ132704) DnaJ1 protein [Anabaena variabilis]; E=2e-39 COG: slr0093; COG2214 Molecular chaperones, DnaJ class; E=9e-41 TP0217; COG0484 Molecular chaperones (contain C-terminal Zn finger; E=2e-27 XF2233; COG2214 Molecular chaperones, DnaJ class; E=1e-26 PFAM: PF00226; DnaJ domain; E=3.6e-37 PF01556; DnaJ C terminal region; E=0.48.
 
 0.851
dnaJ-2
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, D [...]
 
 0.827
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.
  
 
 0.797
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.
  
 
 0.797
groEL
Heat shock protein GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.705
groEL-2
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.705
groEL-3
60 kDa chaperonin 5; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.705
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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