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
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Co-expression
Experiments
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[Homology]
Score
ECA2332Similar to Yersinia pestis hypothetical protein ypo2172/y2149 ypo2172 or y2149 SWALL:AAM85711 (EMBL:AJ414151) (154 aa) fasta scores: E(): 2.7e-36, 56.77% id in 155 aa, and to Shigella flexneri hypothetical protein ychj ychj or sf1233 SWALL:YCHJ_SHIFL (SWALL:P38481) (152 aa) fasta scores: E(): 6.2e-29, 47.74% id in 155 aa; Belongs to the UPF0225 family. (155 aa)    
Predicted Functional Partners:
purU
Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
 
    0.675
expL
Patatin-like phospholipase; Similar to Pectobacterium carotovorum subsp. carotovorum ExpL protein ExpL SWALL:O86196 (EMBL:AJ224437) (303 aa) fasta scores: E(): 1.2e-110, 93.37% id in 302 aa, and to Erwinia chrysanthemi RssA protein RssA SWALL:Q93KA7 (EMBL:AJ410309) (304 aa) fasta scores: E(): 3.1e-84, 72.91% id in 299 aa.
       0.550
secY
Preprotein translocase subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
     
 0.414
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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