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
CAZ95782.1Peptidase family M23 mainly contains endopeptidases that lyze bacterial cell wall peptidoglycans. One catalytic zinc ion is bound per peptidase molecule. The cation ligands occur in the conserved motifs HXXXD and HXH. The first histidine of the second motif is also involved in the catalysis. Contains a transmembrane helix in N-terminus. Localized in the cytoplasmic membrane; Specificity unclear. (288 aa)    
Predicted Functional Partners:
CAZ97280.1
Peptidase family M23 mainly contains endopeptidases that lyze bacterial cell wall peptidoglycans. One catalytic zinc ion is bound per peptidase molecule. The cation ligands occur in the conserved motifs HXXXD and HXH. The first histidine of the second motif is also involved in the catalysis. Features a signal peptide cleaved between the residues 18 and 19. Localized in the periplasm; Specificity unclear.
  
     0.743
CAZ97113.1
Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 26 and 27; Localized in the cytoplasmic and/or outer membrane; Conserved hypothetical protein.
  
   
 0.728
CAZ95783.1
Conserved hypothetical protein distantly related to the Auxin-responsive GH3-like proteins; Localized in the cytoplasm.
       0.577
pbp1A
Penicillin-binding protein 1A, family GT51; Penicillin-binding protein 1A is a class A PBP involved in the synthesis of cross-linked peptidoglycan from the lipid II intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). The N-terminal domain belongs to the family 51 of the glycosyltransferases. Features an uncleaved signal peptide. Localized in the periplasm, anchored to the cytoplasmic membrane; High confidence in [...]
  
   
 0.572
CAZ95784.1
Putative protein.
       0.561
CAZ95827.1
Conserved hypothetical protein belonging to the DUF583 family; Localized in the cytoplasm.
 
   
 0.549
tatA
Sec-independent protein translocase TatA; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
       0.507
exbD1
ExbD is involved in the tonB-dependent energy-dependent transport of various receptor-bound substrates. ExbD forms a complex with ExbB. This complex is required for the efficient energization of tonB from the protomotive force; Contains a N-terminal transmembrane helix; Belongs to the exbD/tolR family; Localized in the cytoplasmic membrane; High confidence in function and specificity.
  
     0.488
CAZ95254.1
TPR repeats protein; Conserved protein containing three tetratrico peptide repeats (TPRs). TPR repeats mediate proteinprotein interactions and the assembly of multiprotein complexes; Signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space; Family membership.
  
     0.479
amiA
N-acetylmuramoyl-L-alanine amidase; The protein contains two domains. A N-terminal N-acetylmuramoyl-L-alanine amidase domain (230 residues) that hydrolyzes the amide bond between N-acetylmuramoyl residues and L-amino acid residues in bacterial cell walls and a C-terminal domain (200 residues) of unknown function; Contains one N-terminal transmembrane segment; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family; Localized in the cytoplasmic membrane; High confidence in function and specificity.
 
  
 0.463
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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