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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
plsXPhosphate:acyl-[acyl carrier protein] acyltransferase; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. (346 aa)    
Predicted Functional Partners:
fabH
3-oxoacyl-[acyl-carrier-protein] synthase III; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family.
  
 0.993
plsY
Acyl-phosphate glycerol-3-phosphate acyltransferase; 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.
 
  
 0.989
rpmF
TIGRFAM: ribosomal protein L32; PFAM: ribosomal L32p protein; KEGG: pat:Patl_2126 ribosomal protein L32; Belongs to the bacterial ribosomal protein bL32 family.
  
  
 0.968
Ping_0194
PFAM: phospholipid/glycerol acyltransferase; KEGG: she:Shewmr4_3788 glycerol-3-phosphate O-acyltransferase; Belongs to the GPAT/DAPAT family.
     
 0.951
Ping_1088
[Acyl-carrier-protein] S-malonyltransferase; TIGRFAM: malonyl CoA-acyl carrier protein transacylase; PFAM: acyl transferase domain protein; KEGG: ppr:PBPRA1194 putative malonyl Coa-acyl carrier protein transacylase.
  
  
 0.931
Ping_1084
PFAM: protein of unknown function DUF177; KEGG: ppr:PBPRA1190 conserved hypothetical protein.
 
    0.919
rplR
LSU ribosomal protein L18P; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
   
    0.873
rpsH
SSU ribosomal protein S8P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
   
    0.870
rplO
LSU ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
   
    0.869
rpsG
SSU ribosomal protein S7P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
   
    0.838
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.