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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
CAZ97856.1Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. (86 aa)    
Predicted Functional Partners:
CAZ97855.1
Sodium/solute symporter; Sodium/substrate symport is a widespread mechanism of solute transport across cytoplasmic membranes of cells. Thereby the energy stored in an inwardly directed electrochemical sodium gradient (sodium motive force, SMF) is used to drive solute accumulation against a concentration gradient; Contains thirteen transmembrane helices; Localized in the cytoplasmic membrane; Family membership; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
 
    0.951
CAZ97974.1
Conserved protein containing a N-terminal cyclic nucleotide-binding domain, a central CBS domain and a C-terminal DUF294 family domain. The cyclic nucleotide-binding domains are composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. CBS (cystathionine-beta-synthase) domains are small intracellular modules that pair together to form a stable globular domain. They bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role making proteins sensitive to adenosyl carrying ligands. DUF294 family proteins are [...]
 
     0.654
CAZ97857.1
UPF0075 family protein; 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.
       0.601
CAZ97858.1
Beta-N-acetylglucosaminidase, family GH3; Beta-N-acetylglucosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-beta-D-glucosaminides. It belongs to the family 3 of the glycoside hydrolases; High confidence in function and specificity.
       0.601
ampG
Protein AmpG is a signal transducer in beta-lactamase induction. It probably acts as a permease in the beta-lactamase induction system and in peptidoglycan recycling. Belongs to the major facilitator superfamily. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity.
       0.601
acs
Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
  
    0.543
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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