STRINGSTRING
STRING protein interaction network
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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
lspASignal peptidase II; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family. (158 aa)    
Predicted Functional Partners:
SMB83503.1
23S rRNA pseudouridine1911/1915/1917 synthase; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family.
 
    0.871
sepF
Cell division inhibitor SepF; Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
       0.813
SMB83481.1
InterPro IPR002942; COGs: COG2302 conserved hypothetical protein contains S4-like domain; KEGG: aoe:Clos_1410 RNA-binding S4 domain-containing protein; SPTR: Putative YlmH protein; SMART: RNA-binding S4; PFAM: RNA-binding S4.
       0.813
SMB83468.1
Hypothetical protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
       0.811
pyrR
Pyrimidine operon attenuation protein / uracil phosphoribosyltransferase; Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant; Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.
  
    0.787
SMB83464.1
KEGG: aoe:Clos_1406 hypothetical protein; SPTR: Putative uncharacterized protein.
       0.786
plsY
Glycerol-3-phosphate acyltransferase PlsY; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
     
 0.755
der
GTP-binding protein; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
       0.750
gpsA
InterPro IPR011128:IPR006109:IPR006168; COGs: COG0240 Glycerol-3-phosphate dehydrogenase; KEGG: aoe:Clos_1401 glycerol-3-phosphate dehydrogenase (NAD(P)(+)); SPTR: Glycerol-3-phosphate dehydrogenase [NAD(P)+]; PFAM: Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminal; Glycerol-3-phosphate dehydrogenase, NAD-dependent, N-terminal; HAMAP: Glycerol-3-phosphate dehydrogenase, NAD-dependent; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
     
 0.748
lgt
Prolipoprotein diacylglyceryl transferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins; Belongs to the Lgt family.
 
   
 0.571
Your Current Organism:
Peptoniphilus asaccharolyticus
NCBI taxonomy Id: 573058
Other names: P. asaccharolyticus DSM 20463, Peptoniphilus asaccharolyticus DSM 20463, Peptoniphilus asaccharolyticus str. DSM 20463, Peptoniphilus asaccharolyticus strain DSM 20463
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.