STRINGSTRING
ANS84067.1 ANS84067.1 lptB lptB lptA lptA lptC lptC apaG apaG ksgA ksgA pdxA pdxA surA surA lptD lptD ANS84454.1 ANS84454.1 ANS84455.1 ANS84455.1 dsbC dsbC ANS84484.1 ANS84484.1 bamD bamD bamA bamA ANS84676.1 ANS84676.1 lptE lptE bamC bamC ppiD ppiD dsbB dsbB ANS85163.1 ANS85163.1 prmB prmB ANS86051.1 ANS86051.1 bamE bamE ANS86183.1 ANS86183.1 ANS86184.1 ANS86184.1 bamB bamB ANS86208.1 ANS86208.1 ANS86332.1 ANS86332.1 ANS86333.1 ANS86333.1 zapD zapD ANS86514.1 ANS86514.1 ANS86515.1 ANS86515.1 rex2 rex2 dsbD dsbD ppiC ppiC
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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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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ANS84067.1Thiol:disulfide interchange protein DsbA; Involved in disulfide-bond formation. Required for the functional maturation of secreted virulence factors. Acts by transferring its disulfide bond to other proteins. Belongs to the thioredoxin family. DsbA subfamily; Contains 1 thioredoxin domain. (200 aa)
lptBLipopolysaccharide export system ATP-binding protein LptB; Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity); Belongs to the ABC transporter superfamily. Outer membrane lipopolysaccharide export (TC 1. B. 42) family; Contains 1 ABC transporter domain; KEGG: vch:VC2528 lipopolysaccharide export system ATP-binding protein; Acting on acid anhydrides; catalyzing transmembrane movement of substances. (241 aa)
lptALipopolysaccharide export system protein LptA; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm. (165 aa)
lptCHypothetical protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. (187 aa)
apaGContains 1 apaG domain. (126 aa)
ksgA16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))- dimethyltransferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. (268 aa)
pdxA4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). (329 aa)
surAPeptidylprolyl isomerase; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. (431 aa)
lptDLPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (790 aa)
ANS84454.1Lipopolysaccharide export system permease protein LptF; Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane; Belongs to the LptF/LptG family. (367 aa)
ANS84455.1Lipopolysaccharide export system permease protein LptG; Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane; Belongs to the LptF/LptG family. (356 aa)
dsbCProtein disulfide-isomerase; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (248 aa)
ANS84484.1Lysophospholipase NTE1; Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (By similarity); Belongs to the NTE family; Contains 2 cyclic nucleotide-binding domains; Contains 1 patatin domain. (760 aa)
bamDOuter membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (241 aa)
bamAOuter membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (800 aa)
ANS84676.1Uncharacterized protein. (248 aa)
lptELPS-assembly lipoprotein LptE; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. (220 aa)
bamCOuter membrane protein assembly factor BamC; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (340 aa)
ppiDPeptidylprolyl isomerase; PPIases accelerate the folding of proteins; Contains 1 PpiC domain; KEGG: vch:VC1918 peptidyl-prolyl cis-trans isomerase D. (619 aa)
dsbBDisulfide bond formation protein B; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (173 aa)
ANS85163.1Thiol:disulfide interchange protein DsbA; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis. Belongs to the thioredoxin family. DsbA subfamily; Contains 1 thioredoxin domain. (206 aa)
prmBRibosomal protein L3 N(5)-glutamine methyltransferase; Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. (310 aa)
ANS86051.1Belongs to the UPF0115 family; Contains 1 Smr domain. (176 aa)
bamEOuter membrane protein assembly factor BamE; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (127 aa)
ANS86183.1Belongs to the UPF0125 (RnfH) family. (117 aa)
ANS86184.1Persistence and stress-resistance toxin PasT; Toxic component of a toxin-antitoxin (TA) module. Binds to 50S ribosomal subunits, preventing them from associating with 30S subunits to form 70S ribosomes (By similarity). In this strain of E. coli low levels of PasT complement operon disruption, however high levels are toxi; their effects are abrogated by high level expression of cognate antitoxin PasI. Plays a role in persistence after antibiotic exposure and survival of nitrosative stres; the toxic and persistence phenotypes are conferred by the same N- terminal region of the protein, w [...] (147 aa)
bamBOuter membrane protein assembly factor BamB; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (386 aa)
ANS86208.1UPF0070 protein YfgM; Belongs to the UPF0070 family. (204 aa)
ANS86332.1Stringent starvation protein; Seems to act in concert with SspA in the regulation of several proteins during exponential and stationary-phase growth. The exact function of SspB is not yet known (By similarity); Belongs to the SspB family. (158 aa)
ANS86333.1Stringent starvation protein; Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme; Belongs to the GST superfamily. HSP26 family; Contains 1 GST C-terminal domain; Contains 1 GST N-terminal domain. (211 aa)
zapDCell division protein ZapD; Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. (246 aa)
ANS86514.1Inner membrane protein YpjD. (264 aa)
ANS86515.1UPF0053 inner membrane protein YfjD; Belongs to the UPF0053 family; Contains 2 CBS domains; Contains 1 DUF21 domain. (424 aa)
rex2Oligoribonuclease; 3'-to-5' exoribonuclease specific for small oligoribonucleotides; Belongs to the oligoribonuclease family. (181 aa)
dsbDProtein-disulfide reductase; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. (601 aa)
ppiCPeptidylprolyl isomerase; PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates (By similarity); Belongs to the PpiC/parvulin rotamase family; Contains 1 PpiC domain; KEGG: eca:ECA4216 peptidyl-prolyl cis-trans isomerase C. (92 aa)
Your Current Organism:
Vibrio scophthalmi
NCBI taxonomy Id: 45658
Other names: CAIM 75, CECT 4638, CIP 105211, LMG 19158, LMG:19158, V. scophthalmi, strain A089
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