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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
ECA1592Putative acetyl-hydrolase; Similar to Streptomyces hygroscopicus acetyl-hydrolase Bah SWALL:BAH_STRHY (SWALL:Q01109) (299 aa) fasta scores: E(): 8.6e-34, 43.01% id in 265 aa, and to Streptomyces viridochromogenes N-acetylphosphinothricin-tripetide- deacetylase Dea SWALL:Q56171 (EMBL:X65195) (299 aa) fasta scores: E(): 1.7e-33, 43.34% id in 263 aa. (300 aa)    
Predicted Functional Partners:
nuoC
NADH-quinone oxidoreductase chain C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
    
   0.870
ECA0705
Partial CDS. Similar to an internal region of Agrobacterium tumefaciens non-ribosomal peptide synthetase MtaD or atu3682 or agr_l_2311 SWALL:Q8U9P4 (EMBL:AE009297) (2399 aa) fasta scores: E(): 0.00074, 32.99% id in 97 aa, and to Anabaena sp. peptide synthetase all2648 SWALL:Q8YTR5 (EMBL:AP003590) (2588 aa) fasta scores: E(): 0.0032, 34.4% id in 93 aa.
  
 
 0.698
ECA1591
Conserved hypothetical protein; Similar over its C-terminal region to many including Salmonella typhimurium putative cytoplasmic protein ybdf or stm0579 SWALL:Q8ZR44 (EMBL:AE008722) (122 aa) fasta scores: E(): 1.8e-09, 33.89% id in 118 aa, and to Escherichia coli, and Escherichia coli O157:H7 hypothetical protein ybdf or b0579 or z0718 or ecs0617 SWALL:YBDF_ECOLI (SWALL:P39454) (122 aa) fasta scores: E(): 2.2e-07, 33.04% id in 115 aa.
       0.689
cfa6
Similar to Pseudomonas syringae type I polyketide synthase Cfa6 SWALL:Q9Z3T9 (EMBL:AF098795) (2731 aa) fasta scores: E(): 0, 60.14% id in 2725 aa, and to Polyangium cellulosum Soraphen polyketide synthase A SorA SWALL:Q9ADL6 (EMBL:U24241) (6315 aa) fasta scores: E(): 0, 43.21% id in 2277 aa.
  
 
 0.679
nuoG
NADH-quinone oxidoreductase chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family.
    
 
 0.602
nuoF
NADH-quinone oxidoreductase chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
    
   0.571
nuoE
NADH-quinone oxidoreductase chain E; Similar to Escherichia coli, Escherichia coli O6, and Shigella flexneri NADH-quinone oxidoreductase chain E NuoE or b2285 or c2826 or sf2361 SWALL:NUOE_ECOLI (SWALL:P33601) (166 aa) fasta scores: E(): 2.7e-53, 84.27% id in 159 aa.
    
   0.564
cfa7
Similar to Pseudomonas syringae type I polyketide synthase Cfa7 SWALL:Q9Z3T8 (EMBL:AF098795) (2066 aa) fasta scores: E(): 0, 52.6% id in 2091 aa, and to Streptomyces coelicolor putative type I polyketide synthase sco6275 SWALL:CAD55506 (EMBL:AL939127) (4557 aa) fasta scores: E(): 3e-183, 44.33% id in 1845 aa.
  
  
 0.522
ECA2694
Putative polyketide synthetase; Similar to Amycolatopsis mediterranei peptide synthetase BpsD SWALL:Q939Y2 (EMBL:Y16952) (581 aa) fasta scores: E(): 2e-44, 32.34% id in 575 aa, and to Myxococcus xanthus Ta1 SWALL:Q9Z5F4 (EMBL:AJ006977) (2393 aa) fasta scores: E(): 4e-51, 32.97% id in 552 aa.
  
  
 0.516
lhr
Similar to Escherichia coli probable ATP-dependent helicase Lhr or RhlF or b1653 SWALL:LHR_ECOLI (SWALL:P30015) (1538 aa) fasta scores: E(): 9.6e-156, 57.39% id in 1603 aa, and to Streptomyces coelicolor ATP dependent DNA helicase sco5761 or sc7c7.16C SWALL:O86821 (EMBL:AL939125) (1690 aa) fasta scores: E(): 3.8e-129, 51.11% id in 1479 aa.
       0.509
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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