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
CAZ97043.1Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Conserved hypothetical protein. (313 aa)    
Predicted Functional Partners:
CAZ97040.1
OmpA-like periplasmic protein; This protein has a modular architecture consisting of a N-terminal TPR motif, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Signal peptide cleaved between the residues 23 and 24; localized in the periplasmic space and/or outer membrane; Family membership.
 
     0.855
CAZ97787.1
OmpA-like periplasmic protein; This protein has a modular architecture with a N-terminal TPR motif, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; localized in the periplasmic space and/or in the outer membrane; Family membership.
 
     0.775
CAZ97790.1
OmpA-like periplasmic protein; This protein has a modular architecture with a N-terminal TPR motif, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane and/or periplasmic space; Family membership.
 
     0.775
CAZ94709.1
OmpA-like outer membrane protein; This protein has a modular architecture with two N-terminal TPR repeats, a central beta-propeller domain, encompassing five WD40 repeats, and a C-terminal OmpA domain. OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions. Signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Function unclear.
 
     0.774
CAZ97221.1
OmpA-like periplasmic protein; This protein has a modular architecture composed of a N-terminal TPR motif, a central beta-propeller domain, encompassing four WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasmic space and/or in the outer membrane; Family membership.
 
     0.763
CAZ95780.1
OmpA-like outer membrane protein; This protein has a modular architecture with a N-terminal domain of unknown function, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. Contains a signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Function unclear.
 
     0.762
CAZ96634.1
Modular protein consisting of a N-terminal domain of unknown function, a central beta-propeller domain, encompassing four WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space or outer membrane; Function unclear.
 
     0.759
gldD
Lipoprotein involved in the gliding motility; Signal peptide cleaved between the residues 17 and 18; localized in the cytoplasmic membrane; Function unclear.
  
     0.747
CAZ98770.1
Protein belonging to the OmpA family. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Localized in the outer membrane; Family membership.
  
     0.739
CAZ96133.1
OmpA-like outer membrane protein; This protein has a modular architecture composed of a N-terminal TPR motif, a central beta-propeller domain, encompassing three WD40 repeats, and a C-terminal OmpA domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan. The tetratrico peptide repeat (TPR) is a structural motif, which mediates proteinprotein interactions; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; Function unclear.
 
     0.734
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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