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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
hsd17b12Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305}; Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long-and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precurso [...] (259 aa)    
Predicted Functional Partners:
tcdA
tRNA threonylcarbamoyladenosine dehydratase; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine; sp|O32037|TCDA_BACSU;evalue=8e-034; PctID=33.74; score=144.
       0.780
SCM57782.1
Putative protein {ECO:0000313|EMBL:CEA16070,1}; tr|A0A098BZF4|A0A098BZF4_9PORP;evalue=7e-112; PctID=47.22; score=410.
       0.509
srlD
Sorbitol-6-phosphate 2-dehydrogenase; sp|P05707|SRLD_ECOLI;evalue=2e-025; PctID=38.66; score=118.
 
 
 0.497
mrdB
Rod shape-determining protein RodA; Required for the maintenance of the rod cell shape. Required for the expression of the enzymatic activity of the penicillin-binding protein 2 (PBP2). protein; sp|P0ABG7|RODA_ECOLI,sp|P0ABG8|RODA_ECO57, sp|P0ABG9|RODA_SHIFL;evalue=5e-029; PctID=43.04; score=129; Belongs to the SEDS family.
  
    0.490
SCM59755.1
UPF0313 protein; sp|Q7MVU9|Y934_PORGI;evalue=0.0; PctID=67.61; score=849.
    0.487
SCM57768.1
Rod shape-determining protein MreC {ECO:0000313|EMBL:CEA16075,1}; tr|A0A098BZF9|A0A098BZF9_9PORP;evalue=1e-081; PctID=54.32; score=309.
       0.472
mreB
Involved in formation of the rod shape of the cell; sp|Q01465|MREB_BACSU;evalue=5e-077; PctID=45.29; score=288.
       0.470
SCM57770.1
Putative membrane protein {ECO:0000313|EMBL:CEA16074,1}; tr|A0A098BZJ0|A0A098BZJ0_9PORP;evalue=1e-032; PctID=51.37; score=145.
       0.470
mrdA
Penicillin-binding protein 2; Cell wall formation; PBP-2 is responsible for the determination of the rod shape of the cell. Its synthesize cross-linked peptidoglycan from the lipid intermediates (By similarity). pass membrane protein (formation of linear glycan strands) and a penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits); sp|E1WGF1|PBP2_SALTS,sp|P0CL14|PBP2_SALTY;evalue=7e-038; PctID=31.78; score=159.
       0.470
alaS-2
Alanine-tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. diphosphate + L-alanyl-tRNA(Ala). Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence=; Note=Binds 1 zinc ion per subunit; domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with [...]
       0.446
Your Current Organism:
Petrimonas mucosa
NCBI taxonomy Id: 1642646
Other names: CECT 8611, DSM 28695, P. mucosa, Petrimonas mucosa Hahnke et al. 2016, Petrimonas sp. ING2-E5A, strain ING2 E5A, strain ING2-E5A
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