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
flgKPMID: 8158647 best DB hits: BLAST: pir:A81293; probable flagellar hook-associated protein Cj1466; E=8e-31 pir:G71853; flagellar hook-associated protein 1 (hap1) -; E=9e-29 gb:AAG61142.1; (AF333079) flagellar hook-associated protein 1; E=2e-28 COG: Cj1466; COG1256 Flagellar hook-associated protein; E=8e-32 PFAM: PF00460; Flagella basal body rod protein; E=7.7e-08. (584 aa)    
Predicted Functional Partners:
flgE
Flagellar hook protein FlgE; PMID: 10368149 best DB hits: BLAST: gb:AAD24206.1; AF049342_4 (AF049342) flagellar hook protein FlgE; E=8e-22 gb:AAA61738.1; (U19712) flagellar hook polypeptide [Borrelia; E=1e-21 gb:AAA91361.1; (U12870) flagellar distal rod protein [Borrelia; E=3e-21 COG: BB0283; COG1749 Flagellar basal body and hook proteins; E=5e-22 PFAM: PF00460; Flagella basal body rod protein; E=3.7e-10.
 
  
 0.997
RB10924
Probable sensor/response regulator hybrid; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family.
  
  
 0.993
RB4511
Sensory transduction histidine kinase; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family.
  
  
 0.993
fliM
Flagellar motor switch protein fliM; PMID: 96345631 PMID: 8755894 best DB hits: BLAST: swissprot:P74927; FLIM_TREPA FLAGELLAR MOTOR SWITCH PROTEIN FLIM; E=7e-47 swissprot:Q57511; FLIM_BORBU FLAGELLAR MOTOR SWITCH PROTEIN FLIM; E=5e-46 ddbj:BAB06165.1; (AP001515) flagellar motor switch protein; E=3e-44 COG: TP0721; COG1868 Flagellar motor switch protein; E=7e-48 PFAM: PF02154; Flagellar motor switch protein FliM; E=1.3e-68 PF01052; Surface presentation of antigens (S; E=0.19.
 
  
 0.981
flgC
Flagellar basal-body rod potein FlgC; PMID: 2129540 PMID: 2404955 PMID: 11677608 best DB hits: BLAST: swissprot:Q57466; FLGC_BORBU FLAGELLAR BASAL-BODY ROD PROTEIN FLGC; E=2e-18 gb:AAC45656.1; (U82214) FlgC [Proteus mirabilis]; E=4e-18 swissprot:P16438; FLGC_SALTY FLAGELLAR BASAL-BODY ROD PROTEIN FLGC; E=1e-17 COG: BB0293; COG1558 Flagellar basal body rod protein; E=2e-19 PFAM: PF00460; Flagella basal body rod protein; E=0.001; Belongs to the flagella basal body rod proteins family.
 
  
 0.981
fliD
Probable lateral flagellar hook-associated protein 2; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
 
  
 0.980
pomA
Chemotaxis pomA protein; PMID: 99254111 best DB hits: BLAST: swissprot:P46826; YTXD_BACME HYPOTHETICAL 29.3 KD PROTEIN IN CCPA; E=9e-35 swissprot:O06873; POMA_VIBAL CHEMOTAXIS POMA PROTEIN -----; E=2e-31 gb:AAD15904.1; (AF069391) sodium-driven polar flagellar protein; E=3e-31 COG: BS_ytxD; COG1291 Flagellar motor component; E=5e-32 PFAM: PF01618; MotA/TolQ/ExbB proton channel famil; E=0.0002.
 
  
 0.980
fliI
Flagellum-specific ATP synthase; PMID: 1828465 best DB hits: BLAST: pir:D72404; flagellum-specific ATP synthase - Thermotoga maritima; E=1e-108 ddbj:BAB06174.1; (AP001515) flagellar-specific ATP synthase; E=1e-106 swissprot:P23445; FLII_BACSU FLAGELLUM-SPECIFIC ATP SYNTHASE; E=1e-103 COG: TM0218; COG1157 Flagellar biosynthesis/type III secretory pathway; E=1e-109 atpD; COG0055 F0F1-type ATP synthase beta subunit; E=2e-37 PFAM: PF00005; ABC transporter; E=0.024 PF00006; ATP synthase alpha/beta family,; E=4e-131.
 
  
 0.979
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.
 
  
 0.979
fliQ
Probable flagellar biosynthetic protein fliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family.
 
  
 0.978
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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