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htpX htpX recF recF TMO_0404 TMO_0404 cutL cutL hspB hspB acoD acoD fliS fliS celY celY flgK flgK flgI flgI flgH flgH flgG flgG flgF flgF fliM fliM fliP fliP csrA csrA flgB flgB flgC flgC fliE fliE yscS yscS fliR fliR flhB flhB recA recA mdtC mdtC cutM cutM cutL-2 cutL-2 fliI fliI TMO_1239 TMO_1239 flhA flhA fliN fliN fliG fliG fliF fliF flgE flgE flgD flgD silP silP surE surE sodB sodB crtB crtB uvrA uvrA TMO_1578 TMO_1578 recO recO recG recG groL groL groS groS ureD ureD ureB ureB ureC ureC ureE ureE ureF ureF ureG ureG copZ copZ recJ recJ phnE phnE phnD phnD phnC phnC recQ recQ copB copB acrA acrA recR recR motB motB hslR hslR htpG htpG trxA trxA trxA-2 trxA-2 ppk ppk maoI maoI hslU hslU hrcA hrcA grpE grpE dnaK dnaK dnaJ dnaJ phoR phoR pstB pstB phoU phoU phoB phoB
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.
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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
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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
Others
textmining
co-expression
protein homology
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htpXHeat shock protein HtpX; Belongs to the peptidase M48B family. (303 aa)
recFRecombination protein F; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. (421 aa)
TMO_0404Glutathione peroxidase; Belongs to the glutathione peroxidase family. (213 aa)
cutLCarbon-monoxide dehydrogenase (acceptor). (773 aa)
hspBSmall heat shock protein; Belongs to the small heat shock protein (HSP20) family. (146 aa)
acoDAcetaldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (515 aa)
fliSFlagellar protein FliS. (158 aa)
celYCellulase. (434 aa)
flgKFlagellar hook-associated protein; Belongs to the flagella basal body rod proteins family. (603 aa)
flgIFlagellar P-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (387 aa)
flgHFlagellar basal body L-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (264 aa)
flgGFlagellar basal-body rod protein FlgG; Belongs to the flagella basal body rod proteins family. (261 aa)
flgFFlagellar basal-body rod protein; Belongs to the flagella basal body rod proteins family. (250 aa)
fliMFlagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. (368 aa)
fliPFlagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (256 aa)
csrACarbon storage regulator; A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW. (87 aa)
flgBFlagellar basal body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (140 aa)
flgCFlagellar basal-body rod protein FlgC. (135 aa)
fliEFlagellar hook-basal body complex protein FliE. (104 aa)
yscSFlagellar biosynthetic protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (91 aa)
fliRFlagellar biosynthesis protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (251 aa)
flhBFlagellar biosynthetic protein FlhB; 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. (359 aa)
recARecA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. (366 aa)
mdtCAcrB; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. (998 aa)
cutMCarbon-monoxide dehydrogenase (acceptor). (266 aa)
cutL-2Carbon monoxide dehydrogenase large chain. (795 aa)
fliIFlagellum-specific ATP synthase. (445 aa)
TMO_1239FlhF. (440 aa)
flhAFlagellar biosynthesis pathway, component FlhA; 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. (707 aa)
fliNFlagellar motor switch protein; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. (117 aa)
fliGFlagellar motor switch protein G; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. (340 aa)
fliFFlagellar MS-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (568 aa)
flgEFlagellar hook protein flgE. (567 aa)
flgDFlagellar basal-body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein. (259 aa)
silPCation transport ATPase. (697 aa)
surEAcid phosphatase; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. (251 aa)
sodBSuperoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (199 aa)
crtBFusion protein of y4aC and y4aD. (594 aa)
uvrAExcinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. (963 aa)
TMO_1578Aldehyde Dehydrogenase; Belongs to the aldehyde dehydrogenase family. (530 aa)
recODNA repair protein RecO; Involved in DNA repair and RecF pathway recombination. (262 aa)
recGATP-dependent DNA helicase. (699 aa)
groLGroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
groSChaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
ureDUrease accessory protein UreD; Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. (318 aa)
ureBUrease subunit beta; Belongs to the urease beta subunit family. (132 aa)
ureCUrease alpha subunit. (569 aa)
ureEUrease accessory protein; Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (281 aa)
ureFUrease accessory protein UreF; Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. (251 aa)
ureGUrease accessory protein; Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. (219 aa)
copZHeavy metal transport/detoxification protein. (69 aa)
recJsingle-stranded-DNA-specific exonuclease. (596 aa)
phnEPhosphonate ABC transporter, inner membrane subunit. (268 aa)
phnDBinding protein component of ABC phosphonate transporter. (344 aa)
phnCPhosphonates ABC transporter, ATP-binding protein; Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system; Belongs to the ABC transporter superfamily. Phosphonates importer (TC 3.A.1.9.1) family. (284 aa)
recQATP-dependent DNA helicase. (552 aa)
copBCopper resistance B precursor. (230 aa)
acrASecretion protein HlyD; Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. (412 aa)
recRRecombinational DNA repair protein (RecF pathway); May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. (199 aa)
motBChemotaxis MotB protein. (349 aa)
hslRHeat shock protein. (144 aa)
htpGChaperone protein htpG; Molecular chaperone. Has ATPase activity. (648 aa)
trxAThioredoxin. (305 aa)
trxA-2Thioredoxin 1; Belongs to the thioredoxin family. (107 aa)
ppkPolyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (795 aa)
maoITyramine oxidase. (640 aa)
hslUATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. (437 aa)
hrcATranscriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (376 aa)
grpEGrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] (206 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (642 aa)
dnaJChaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (393 aa)
phoRTwo-component sensor histidine kinase. (480 aa)
pstBPhosphate import ATP-binding protein; Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system; Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family. (256 aa)
phoUPhosphate transport system protein PhoU; Plays a role in the regulation of phosphate uptake. (241 aa)
phoBResponse regulator. (232 aa)
Your Current Organism:
Tistrella mobilis
NCBI taxonomy Id: 1110502
Other names: T. mobilis KA081020-065, Tistrella mobilis KA081020-065, Tistrella mobilis str. KA081020-065, Tistrella mobilis strain KA081020-065
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