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.
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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.
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from curated databases
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experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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csrAProbable CsrA_thema carbon storage regulator homolog; A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW. (81 aa)    
Predicted Functional Partners:
csrA-3
Probable carbon storage regulator; A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW.
  
  
  0.976
fliW
Conserved hypothetical protein; Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
 
 
 0.873
bfr
Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.
   
  
 0.628
RB1753
Conserved hypothetical protein; PMID: 10960085 best DB hits: BLAST: embl:CAB95035.1; (AJ272497) orf4 [Bacillus anthracis]; E=9e-12 pir:B83036; probable bacterioferritin PA4880 [imported] -; E=0.005 pir:G82332; bacterioferritin VC0365 [imported] - Vibrio cholerae; E=0.019 COG: PA4880; COG2193 Bacterioferritin (cytochrome b1); E=5e-04.
   
  
 0.628
eIF-2B
Putative translation initiation factor eIF-2B; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
 
     0.474
RB10263
Hypothetical protein.
       0.446
fliF
Probable polar flagellar M-ring protein FliF; PMID: 20115548 PMID: 10648530 best DB hits: BLAST: gb:AAD15920.1; (AF069392) polar flagellar M-ring protein FliF; E=6e-04 swissprot:Q53151; FLIF_RHOSH FLAGELLAR M-RING PROTEIN -----; E=0.001 swissprot:O67241; FLIF_AQUAE FLAGELLAR M-RING PROTEIN -----; E=0.002 COG: aq_1182; COG1766 Flagellar biosynthesis/type III secretory pathway; E=2e-04 PFAM: PF01514; Secretory protein of YscJ/FliF fa; E=0.00027.
  
  
 0.419
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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