STRINGSTRING
cwlD cwlD ydcC ydcC rbn rbn pdaA pdaA yheD yheD cotZ cotZ spoVD spoVD spoVE spoVE ftsZ ftsZ spoVM spoVM cotE cotE spoIVA spoIVA spoIIM spoIIM spo0A spo0A spoIIIAH spoIIIAH spoIIIAG spoIIIAG spoIIP spoIIP rarA rarA safA safA spoIVFB spoIVFB spoIVFA spoIVFA mreB mreB spoVID spoVID yutH yutH spoIIQ spoIIQ spoIID spoIID rpoE rpoE
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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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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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cwlDN-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex. (237 aa)
ydcCPutative lipoprotein; required for efficient sporulation. (338 aa)
rbnPutative ribonuclease BN; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (275 aa)
pdaAExported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family. (263 aa)
yheDSpore coat associated protein; Involved in sporulation. (453 aa)
cotZSpore coat protein (insoluble fraction, outermost layer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (148 aa)
spoVDPenicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell. (646 aa)
spoVEFactor for spore cortex peptidoglycan synthesis (stage V sporulation); May play an essential role not only during sporulation, but also during vegetative growth; Belongs to the SEDS family. SpoVE subfamily. (366 aa)
ftsZCell-division initiation protein; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. (382 aa)
spoVMFactor required for normal spore cortex and coat synthesis (stage V sporulation); Coordinates cortex and coat assembly during sporulation. Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface. May also serve as a competitive inhibitor of FtsH activity during sporulation. (26 aa)
cotEMorphogenic spore protein; Morphogenic protein required for the assembly of the outer coat of the endospore. Is also a regulatory protein for the expression of cotA, cotB, cotC, cotH and other genes encoding spore outer coat proteins. (181 aa)
spoIVAMorphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM. (492 aa)
spoIIMAutolysin component for dissolution of the septal cell wall (stage II sporulation); Required for complete septum migration and engulfment of the forespore compartment during sporulation. Required for stabilizing and recruiting of SpoIIP to the septal membrane. (214 aa)
spo0AResponse regulator; May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box). (267 aa)
spoIIIAHStage III sporulation ratchet engulfment protein; Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling. (218 aa)
spoIIIAGStage III sporulation engulfment assembly protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (229 aa)
spoIIPSpore autolysin (stage II sporulation); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (401 aa)
rarADNA-dependent ATPase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily. (421 aa)
safAMorphogenetic protein associated with SpoVID; Probably involved in the assembly of some coat protein components implicated in both lysozyme resistance and germination. Could be required for the assembly of CotG. Associates with SpoIVD during the early stage of coat assembly. (387 aa)
spoIVFBMembrane metalloprotease; Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor. (288 aa)
spoIVFARegulator of SpoIVFB (stage IV sporulation); Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation at 37 degrees Celsius, but not at 30 degrees Celsius. SpoIVFA plays a central role in both maintaining the SpoIVFA/BofA/SpoIVFB complex and anchoring it to the outer forespore membrane. SpoIVFA brings BofA into close proximity to SpoIVFB, allowing BofA to inhibit SpoIVFB. Increased accumulation of SpoIVFA seems to inhibit the activity of SpoIVFB and thus regulates the activation of sigma-K. (264 aa)
mreBCell-shape determining protein; Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polymerization. The [...] (337 aa)
spoVIDMorphogenetic spore protein (stage VI sporulation); Required for assembly of a normal spore coat. May be a component of the innermost layer of the spore coat that aids in its adherence to the prespore. (575 aa)
yutHSpore coat-associated protein; Involved in sporulation; Belongs to the CotS family. (339 aa)
spoIIQForespore protein required for alternative engulfment; Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling. (283 aa)
spoIIDAutolysin required for complete dissolution of the asymmetric septum (stage II sporulation); May act at the level of sigma-G activity or its stability. SpoIID is probably required for engulfment. (343 aa)
rpoERNA polymerase (delta subunit); Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. May function in sigma factor switching. It displaces RNA bound to RNA polymerase in a binary complex; Belongs to the RpoE family. (173 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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