STRINGSTRING
RB9276 RB9276 flgK flgK flgI flgI flgH flgH flgG flgG flgF flgF flgE flgE fliQ fliQ fliD fliD fliC fliC FliC FliC flgL flgL fliC-2 fliC-2 flgC flgC fliE fliE
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:
RB9276Flagellar protein; Best DB hits: BLAST: swissprot:P49080; AKH2_MAIZE BIFUNCTIONAL ASPARTOKINASEHOMOSERINE; E=0.43. (233 aa)
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)
flgIFlagellar P-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (379 aa)
flgHProbable flagellar L-ring protein precursor FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (301 aa)
flgGPMID: 2129540 best DB hits: BLAST: pir:C70372; flagellar hook basal body protein flgG - Aquifex; E=3e-55 pir:A64718; flagellar basal body rod protein flgG - Helicobacter; E=2e-51 pir:F71801; flagellar basal-body rod protein (distal rod protein) -; E=4e-51 COG: aq_834; COG1749 Flagellar basal body and hook proteins; E=2e-56 PFAM: PF00460; Flagella basal body rod protein; E=4.1e-13. (268 aa)
flgFFlgF; PMID: 10411267 best DB hits: BLAST: gb:AAB71784.1; (U95165) FlgF [Agrobacterium tumefaciens]; E=1e-17 ddbj:BAB06168.1; (AP001515) flagellar hook protein [Bacillus; E=1e-16 swissprot:Q06171; FLGF_CAUCR FLAGELLAR BASAL-BODY ROD PROTEIN FLGF; E=3e-16 COG: BH2449; COG1749 Flagellar basal body and hook proteins; E=1e-17 PFAM: PF00460; Flagella basal body rod protein; E=0.00036. (273 aa)
flgEFlagellar 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. (811 aa)
fliQProbable flagellar biosynthetic protein fliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (88 aa)
fliDProbable 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. (793 aa)
fliCFlagellin E; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (718 aa)
FliCFlagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (739 aa)
flgLProbable flagellar hook-associated protein 3; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (651 aa)
fliC-2Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (685 aa)
flgCFlagellar 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. (143 aa)
fliEPMID: 1905667 best DB hits: BLAST: pir:G72263; flagellar hook-basal body complex protein FliE -; E=7e-05 swissprot:O67242; FLIE_AQUAE FLAGELLAR HOOK-BASAL BODY COMPLEX; E=1e-04 pir:E64714; flagellar hook-basal body complex protein - Helicobacter; E=0.002 COG: TM1366; COG1677 Flagellar hook-basal body protein; E=7e-06 PFAM: PF02049; Flagellar hook-basal body complex pr; E=1.9e-12. (139 aa)
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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