STRINGSTRING
gbpA gbpA anmK anmK nagZ nagZ chb chb CED70136.1 CED70136.1 glmS glmS nagB nagB CED70541.1 CED70541.1 chbP chbP exoI exoI CED70544.1 CED70544.1 CED70545.1 CED70545.1 glmM glmM nagA nagA hexR hexR CED71069.1 CED71069.1 murQ murQ CED71336.1 CED71336.1 chiA chiA glmU glmU
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:
gbpAGlcNAc-binding protein A; Probably interacts with GlcNAc residues. May promote attachment to both epithelial cell surfaces and chitin. Belongs to the GbpA family. (491 aa)
anmKanhydro-N-acetylmuramic acid kinase; Catalyzes the specific phosphorylation of 1,6-anhydro-N- acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling; Belongs to the anhydro-N-acetylmuramic acid kinase family. (367 aa)
nagZBeta-hexosaminidase (beta-N-acetylhexosaminidase); Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide- linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N- acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Belongs to the glycosyl hydrolase 3 family. NagZ subfamily. (331 aa)
chbN,N'-diacetylchitobiase (chitobiase). (881 aa)
CED70136.1Putative beta-N-acetylhexosaminidase. (815 aa)
glmSGlucosamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (610 aa)
nagBGlucosamine-6-phosphate deaminase; Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. (266 aa)
CED70541.1Phosphoglucomutase/phosphomannomutase. (470 aa)
chbPChitobiose phosphorylase (glycosyl transferase). (801 aa)
exoIBeta-hexosaminidase (beta-N-acetylglucosaminidase). (634 aa)
CED70544.1Glucosamine kinase. (291 aa)
CED70545.1Putative endochitinase. (572 aa)
glmMPhosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the phosphohexose mutase family. (445 aa)
nagAN-acetylglucosamine-6-phosphate deacetylase. (378 aa)
hexRHTH-type transcriptional regulator HexR. (284 aa)
CED71069.1Chitodextrinase. (1055 aa)
murQN-acetylmuramic acid 6-phosphate etherase; Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. (298 aa)
CED71336.1Chitinase. (569 aa)
chiAChitinase. (845 aa)
glmUBifunctional protein GlmU; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. (453 aa)
Your Current Organism:
Aliivibrio wodanis
NCBI taxonomy Id: 80852
Other names: A. wodanis, ATCC BAA-104, Aliivibrio wodanis (Lunder et al. 2000) Urbanczyk et al. 2007, DSM 22225, LMG 24053, LMG:24053, NCIMB 13582, Vibrio wodanis, Vibrio wodanis Lunder et al. 2000, strain NVI 88/441
Server load: medium (56%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.