STRINGSTRING
flaA flaA cdtC cdtC cdtB cdtB cdtA cdtA glyA glyA pgm pgm glnA glnA ciaB ciaB hipO hipO cheY cheY dnaJ dnaJ cadF cadF tkt tkt gltA gltA
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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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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flaAFlagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaA binds to flagellar assembly factor FliW protein, preventing FliW from binding to CsrA, so that CsrA can then bind flaA mRNA and represses its translation. (572 aa)
cdtCOriginal (2000) note: Cj0077c, cdtC, cytolethal distending toxin, len: 189 aa, identical to TR:Q46102 (EMBL:U51121) cdtC (189 aa). No Hp match. Contains N-terminal signal sequence; Updated (2006) note: Pfam domain PF03499 Cytolethal distending toxin C identified within CDS. Product modified to more specific family member due to motif match. Characterised within Campylobacter jejuni, so putative not added to product function. Functional classification -Pathogenicity; PMID:10688204, PMID:8675309, PMID:11083762. (189 aa)
cdtBOriginal (2000) note: Cj0078c, cdtB, cytolethal distending toxin, len: 265 aa; identical toTR:Q46101 (EMBL:U51121) cdtB (265 aa) and similar to e.g. TR:Q47089 (EMBL:U03293) Escherichia coli cdtB (273 aa), fasta scores; opt: 946 z-score: 1533.6 E(): 0, 55.2% identity in 268 aa overlap. No Hp match. Contains N-terminal signal sequence; Updated (2006) note: Prosite domain PRO1388 CDTOXINB, Cytolethal distending toxin B signature identified within CDS. Product modified to more specific family member due to motif match. Characterised within Campylobacter jejuni, so putative not added to pro [...] (265 aa)
cdtACytolethal distending toxin A; CDTs are cytotoxins which induce cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. (268 aa)
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity). (414 aa)
pgm2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (492 aa)
glnAGlutamine synthetase; Original (2000) note: Cj0699c, glnA, probable glutamine synthetase, len: 476 aa; highly similar to many e.g. GLNA_ECOLI glutamine synthetase (EC 6.3.1.2) (468 aa), fasta scores; opt: 1529 z-score: 1812.8 E(): 0,51.5% identity in 462 aa overlap. 63.6% identity to HP0512. Contains PS00180 Glutamine synthetase signature 1,PS00181 Glutamine synthetase putative ATP-binding region signature, and Pfam match to entry PF00120 gln-synt; Updated (2006) note: Characterised within Escherichia coli with acceptable identity score. Putative not added to product function. Function [...] (476 aa)
ciaBCiaB protein; Original (2000) note: Cj0914c, ciaB, unknown function, len: 610 aa; no Hp match. Product is translocated into host cells. Mutants fail to translocate,and fail to translocate other proteins. Contains PS00142 Neutral zinc metallopeptidases, zinc-binding region signature; Updated (2006) note: Papers attached giving further information regarding this CDS. Functional classification - Pathogenicity; PMID:10361274, PMID:10540297, PMID:10659361,PMID:15722140. (610 aa)
hipOHippurate hydrolase; Cleaves hippuric acid into benzoic acid and glycine. Belongs to the peptidase M20 family. (383 aa)
cheYChemotaxis regulatory protein; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheY seems to regulate the clockwise (CW) rotation (By similarity). (130 aa)
dnaJChaperone 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, DnaK and [...] (373 aa)
cadFOriginal (2000) note: Cj1478c, cadF, outer membrane fibronectin-binding protein, len: 319 aa; 82.8% identical to TR:O06895 (EMBL:U87559) C. jejuni CADF precursor (fibronectin-binding protein) (326 aa), and similar to many oprF proteins e.g. PORF_PSEFL outer membrane porin F precursor (root adhesin) (326 aa), fasta scores; opt: 401 z-score: 458.6 E(): 3.2e-18, 29.1% identity in 316 aa overlap. No Hp match. Contains PS01068 OmpA-like domain,and Pfam match to entry PF00691 OmpA, OmpA family; Updated (2006) note: Characterised within Campylobacter jejuni, so putative not added to product f [...] (319 aa)
tktTransketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. (632 aa)
gltACitrate synthase; Original (2000) note: Cj1682c, gltA, probable citrate synthase, len: 422 aa; similar to many e.g. CISY_PSEAE citrate synthase (EC 4.1.3.7) (428 aa), fasta scores; opt: 1520 z-score: 1734.6 E(): 0, 53.8% identity in 405 aa overlap. 52.8% identity to HP0026. Contains PS00480 Citrate synthase signature, and Pfam match to entry PF00285 citrate_synt, Citrate synthase; Updated (2006) note: Characterised within Pseudomonas aeruginosa with acceptable identity score. Appropriate motifs present. Putative not added to product function. EC number has been updated. Functional clas [...] (422 aa)
Your Current Organism:
Campylobacter jejuni NCTC 11168
NCBI taxonomy Id: 192222
Other names: C. jejuni subsp. jejuni NCTC 11168 = ATCC 700819, Campylobacter jejuni subsp. jejuni ATCC 700819, Campylobacter jejuni subsp. jejuni ATCC 700819 = NCTC 11168, Campylobacter jejuni subsp. jejuni NCTC 11168, Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
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