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lfhB lfhB lfhA lfhA flgH flgH mltA mltA A4SMD8_AERS4 A4SMD8_AERS4 nlpB nlpB metQ metQ lptD lptD bamA bamA lfgH lfgH ompC ompC oprC oprC flgE flgE flaA flaA fliD fliD secD secD nlpI nlpI bamB bamB rlpA rlpA btuB btuB nlpD nlpD nlpC nlpC hslJ hslJ blc blc bamD bamD glpC glpC tolC tolC secD-2 secD-2 dnaK dnaK rlpB rlpB rlpA-2 rlpA-2 lolD lolD pqiB pqiB ompA ompA mltC mltC tolC-2 tolC-2 flhA flhA flhB flhB fliR fliR fliQ fliQ fliP fliP fliF fliF lptA lptA lfiP lfiP
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:
lfhBUnannotated protein; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family. (378 aa)
lfhAUnannotated protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (691 aa)
flgHUnannotated protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (223 aa)
mltAUnannotated protein. (383 aa)
A4SMD8_AERS4Unannotated protein; Belongs to the peptidase S41A family. (671 aa)
nlpBUnannotated protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (341 aa)
metQUnannotated protein; Belongs to the nlpA lipoprotein family. (266 aa)
lptDUnannotated protein; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (810 aa)
bamAUnannotated protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (807 aa)
lfgHUnannotated protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (223 aa)
ompCUnannotated protein. (361 aa)
oprCUnannotated protein. (655 aa)
flgEUnannotated protein. (446 aa)
flaAUnannotated protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (305 aa)
fliDUnannotated protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. (464 aa)
secDUnannotated protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (617 aa)
nlpIUnannotated protein; May be involved in cell division. (315 aa)
bamBUnannotated protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (394 aa)
rlpAUnannotated protein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. (135 aa)
btuBUnannotated protein; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. (611 aa)
nlpDUnannotated protein. (348 aa)
nlpCUnannotated protein. (166 aa)
hslJUnannotated protein. (139 aa)
blcUnannotated protein; Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids. (170 aa)
bamDUnannotated protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (254 aa)
glpCUnannotated protein. (400 aa)
tolCUnannotated protein. (441 aa)
secD-2Unannotated protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (600 aa)
dnaKUnannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (641 aa)
rlpBUnannotated protein; 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. (160 aa)
rlpA-2Unannotated protein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. (316 aa)
lolDUnannotated protein; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. (232 aa)
pqiBUnannotated protein. (548 aa)
ompAUnannotated protein; Belongs to the outer membrane OOP (TC 1.B.6) superfamily. (343 aa)
mltCUnannotated protein; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. (366 aa)
tolC-2Unannotated protein. (441 aa)
flhAUnannotated protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (700 aa)
flhBUnannotated protein. (281 aa)
fliRUnannotated protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (265 aa)
fliQUnannotated protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliPUnannotated protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (249 aa)
fliFUnannotated protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (569 aa)
lptAUnannotated protein; 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. (180 aa)
lfiPUnannotated protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (244 aa)
Your Current Organism:
Aeromonas salmonicida
NCBI taxonomy Id: 29491
Other names: A. salmonicida subsp. salmonicida, Aeromonas salmonicida salmonicida, Aeromonas salmonicida subsp. salmonicida
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