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aprE aprE yddN yddN phrI phrI rapI rapI nprE nprE yddJ yddJ ydcR ydcR xylR xylR abrB abrB alrA alrA ndoA ndoA immR immR wprA wprA araR araR thrC thrC cdd cdd alrB alrB xylA xylA comK comK ung ung narI narI upp upp
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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
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:
aprESerine alkaline protease (subtilisin E); Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides; Belongs to the peptidase S8 family. (381 aa)
yddNPutative alkanal monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; To bacterial alkanal monooxygenase alpha and beta chains. (339 aa)
phrISecreted regulator of the activity of phosphatase RapI; Inhibitor of the activity of phosphatase RapI. (39 aa)
rapIResponse regulator aspartate phosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type r: regulator; Belongs to the RAP family. (391 aa)
nprEExtracellular neutral metalloprotease; Extracellular zinc metalloprotease; Belongs to the peptidase M4 family. (521 aa)
yddJPutative lipoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type lp: lipoprotein. (126 aa)
ydcRPutative replication protein; Probable DNA relaxase involved in the transfer of the integrative and conjugative element ICEBs1. Required for the transfer of ICEBs1. Probably mediates conjugation of ICEBs1 by nicking at oriT on the conjugative element and facilitates the translocation of a single strand of ICEBs1 DNA through a transmembrane conjugation pore into the recipient cell; Belongs to the plasmid replication initiation factor family. (352 aa)
xylRTranscriptional regulator; Transcriptional repressor of xylose-utilizing enzymes. (384 aa)
abrBTranscriptional regulator for transition state genes; Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription; To B.subtilis Abh and SpoVT. (96 aa)
alrAD-alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (389 aa)
ndoAEndoribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U. Yields cleavage products with 3' phosphate and 5' hydroxyl groups. Cannot digest substrate with a UUdUACAUAA cleavage site. Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter. (116 aa)
immRPhage element (ICEBs1)transcriptional regulator (Xre family); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin. (127 aa)
wprACell wall-associated protease; CWBP52 is a serine-type protease that could be involved in proteoglycan peptide bridges; Belongs to the peptidase S8 family. (894 aa)
araRTranscriptional repressor of the ara regulon (LacI family); Transcriptional repressor of the arabinose utilization genes. Also regulates its own expression. Binds to two sequences within the promoters of the araABDLMNPQ-abfA operon and the araE gene, and to one sequence in the araR promoter. (362 aa)
thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa)
cddCytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. (136 aa)
alrBAlanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (394 aa)
xylAXylose isomerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the xylose isomerase family. (445 aa)
comKCompetence transcription factor (CTF); A master regulator required for the expression of late competence genes including comC, comE, comG and the bdbDC operon. Receives signals from SrfA, and possibly other regulatory COM genes, and transduces these signals to the late COM genes. Represses transcription of rok. May repress expression of a few genes. (192 aa)
unguracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine; Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family. (225 aa)
narINitrate reductase (gamma subunit); The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. (223 aa)
uppUracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. (209 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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