STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
DR97_1891annotation not available (125 aa)    
Predicted Functional Partners:
annotation not available
Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore
May be involved in the polymerization of mannuronate to alginate
annotation not available
Catalyzes the epimerization of beta-D-mannuronate to alpha-L- guluronate during the synthesis of the linear polysaccharide alginate . In addition, is part of a periplasmic protein complex that protects alginate from degradation by AlgL by channeling the newly formed alginate polymer through a scaffold that transfers the alginate polymer through the periplasmic space to the outer membrane secretin AlgE (PubMed:12581364, PubMed:15968068). ECO:0000269|PubMed:15968068, ECO:0000269|PubMed:16866359,
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity)
Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism (PubMed:8370530, PubMed:8335634, PubMed:23215237). May serve to degrade mislocalized alginate that is trapped in the periplasmic space. Acts preferentially on non-acetylated alginate or its precursor mannuronan. Is able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate. Exhaustive digestion of alginate by AlgL generates dimeric and trimeric products . In addition to its enzymatic function, AlgL appe [...]
Required for alginate biosynthesis.
Uncharacterized protein
Together with AlgI and AlgJ, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
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