STRINGSTRING
luxS luxS flgD flgD cdtC cdtC cdtB cdtB cdtA cdtA motB motB fliD fliD ciaB ciaB csrA csrA pseE pseE flaB flaB flaA flaA pldA pldA ceuE ceuE cadF cadF Cj1556 Cj1556
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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
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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
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
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textmining
co-expression
protein homology
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luxSS-ribosylhomocysteine lyase (autoinducer-2 production protein LuxS); Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. (164 aa)
flgDPutative flagellar hook assembly protein; Required for flagellar hook formation. May act as a scaffolding protein. (294 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)
motBOriginal (2000) note: Cj0336c, motB, possible flagellar motor protein, len: 247 aa; similar to MOTB_BACSU chemotaxis motB protein (motility protein B) (261 aa), fasta scores; opt: 195 z-score: 275.7 E(): 4.2e-08, 30.7% identity in 261 aa overlap. 43.3% identity to HP0816. Contains Pfam match to entry PF00691 OmpA, OmpA family, score 28.50, E-value 5.6e-07; Updated (2006) note: One probable transmembrace helices identified by TMHMM2.0 within CDS. Some characterisation within Bacillus subtilis with marginal identity score. Putative kept within product function. Functional classification [...] (247 aa)
fliDFlagellar hook-associated protein; Required for the 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 (By similarity). (642 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)
csrACarbon 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. Binds mRNA; 77% of enriched bound RNA is for flagellin A (flaA) while another 13% encodes other flagellar or motility-related genes. Binds mRNA in 5'-UTR or intergenic regions, binds consensus 5'-AAGGA-3' in the loop of a predicted stem-loop structure. Binds at least 2 sites in the 5'-UTR of flaA mRNA and represses its translation [...] (75 aa)
pseEPseE protein; Original (2000) note: Cj1337, unknown, len: 628 aa; 35.0% identity to HP0114. A member of the 1318 family of proteins. Simlar to Cj1333 (48.6% identity in 636 aa overlap), Cj1318 (48.1% identity in 643 aa overlap),Cj1336 (48.6% identity in 586 aa overlap), Cj1334 (43.6% identity in 628 aa overlap), Cj1340c (32.2% identity in 624 aa overlap), Cj1341c (31.9% identity in 627 aa overlap); Updated (2006) note: Pfam domain PF01973 Protein of unknown function DUF115 identified within CDS. Some characterisation work carried out within Campylobacter jejuni. Product function modifi [...] (628 aa)
flaBFlagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (572 aa)
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)
pldAPhospholipase A; Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Belongs to the phospholipase A1 family. (329 aa)
ceuEOriginal (2000) note: Cj1355, ceuE, probable enterochelin uptake periplasmic binding protein, len: 330 aa; highly similar to TR:Q46006 (EMBL:X88849) Campylobacter coli ceuE (328 aa), fasta scores; opt: 1903 z-score: 2111.3 E(): 0, 90.6% identity in 330 aa overlap,and similar to e.g. FATB_VIBAN ferric anguibactin-binding protein precursor (322 aa), fasta scores; opt: 540 z-score: 605.4 E(): 2e-26, 30.1% identity in 279 aa overlap. No Hp match. Contains probable N-terminal signal sequence and appropriately positioned PS00013 Prokaryotic membrane lipoprotein lipid attachment site; Updated [...] (330 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)
Cj1556Putative transcriptional regulator; Original (2000) note: Cj1556, unknown, len: 110 aa; similar to hypothetical proteins e.g. YYBR_BACSU (125 aa),fasta scores; opt: 307 z-score: 402.3 E(): 4.3e-15, 43.7% identity in 103 aa overlap. No Hp match. Also similar to Cj1546 (43.6% identity in 101 aa overlap); Updated (2006) note: Pfam domain PF01638 Transcriptional regulator identified within CDS. Product modified to more specific family member based on motif match. No specific characterisation has been carried out yet, so putative kept within product function. Functional classification - Bro [...] (110 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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