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Csal_0033 Csal_0033 Csal_0126 Csal_0126 Csal_0176 Csal_0176 Csal_0506 Csal_0506 Csal_0906 Csal_0906 Csal_1099 Csal_1099 Csal_1504 Csal_1504 Csal_1505 Csal_1505 Csal_1726 Csal_1726 fliE fliE Csal_1955 Csal_1955 Csal_1956 Csal_1956 Csal_1957 Csal_1957 Csal_1958 Csal_1958 Csal_1959 Csal_1959 Csal_1960 Csal_1960 Csal_1961 Csal_1961 Csal_1962 Csal_1962 Csal_1963 Csal_1963 Csal_1964 Csal_1964 fliP fliP fliQ fliQ Csal_1967 Csal_1967 Csal_1968 Csal_1968 flgK flgK Csal_1970 Csal_1970 flgI flgI flgH flgH Csal_1973 Csal_1973 Csal_1974 Csal_1974 Csal_1975 Csal_1975 Csal_1976 Csal_1976 Csal_1977 Csal_1977 Csal_1978 Csal_1978 Csal_1979 Csal_1979 Csal_1980 Csal_1980 Csal_1981 Csal_1981 Csal_1985 Csal_1985 Csal_1989 Csal_1989 fliA fliA Csal_2014 Csal_2014 flhA flhA flhB flhB Csal_2017 Csal_2017 Csal_2018 Csal_2018 Csal_2019 Csal_2019 cheB cheB Csal_2021 Csal_2021 Csal_2022 Csal_2022 Csal_2023 Csal_2023 Csal_2024 Csal_2024 Csal_2025 Csal_2025 Csal_2026 Csal_2026 flhC flhC flhD flhD Csal_2029 Csal_2029 Csal_2030 Csal_2030 Csal_2031 Csal_2031 Csal_2032 Csal_2032 Csal_2033 Csal_2033 Csal_2778 Csal_2778
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:
Csal_0033Methyl-accepting chemotaxis sensory transducer. (593 aa)
Csal_0126Methyl-accepting chemotaxis sensory transducer. (613 aa)
Csal_0176Methyl-accepting chemotaxis sensory transducer. (427 aa)
Csal_0506Flagellar hook-associated 2-like 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. (441 aa)
Csal_0906Methyl-accepting chemotaxis sensory transducer with Pas/Pac sensor. (440 aa)
Csal_1099Methyl-accepting chemotaxis sensory transducer. (699 aa)
Csal_1504OmpA/MotB. (283 aa)
Csal_1505MotA/TolQ/ExbB proton channel. (299 aa)
Csal_1726Methyl-accepting chemotaxis sensory transducer. (702 aa)
fliEFlagellar hook-basal body complex protein (FliE). (107 aa)
Csal_1955Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (594 aa)
Csal_1956Flagellar motor switch protein FliG; 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. (331 aa)
Csal_1957Flagellar assembly protein FliH. (252 aa)
Csal_1958ATPase FliI/YscN. (468 aa)
Csal_1959Flagellar export FliJ. (165 aa)
Csal_1960Flagellar hook-length control protein. (456 aa)
Csal_1961Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (165 aa)
Csal_1962Flagellar 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. (338 aa)
Csal_1963Flagellar motor switch FliN; 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. (175 aa)
Csal_1964Flagellar biosynthesis protein, FliO. (163 aa)
fliPFlagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (249 aa)
fliQFlagellar biosynthetic protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
Csal_1967Flagellar biosynthetic protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (261 aa)
Csal_1968Flagellin-like protein. (410 aa)
flgKFlagellar hook-associated protein. (539 aa)
Csal_1970Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase. (370 aa)
flgIFlagellar P-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (369 aa)
flgHFlagellar L-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (224 aa)
Csal_1973Flagellar basal-body rod FlgG; Belongs to the flagella basal body rod proteins family. (260 aa)
Csal_1974Flagellar basal-body rod FlgF. (253 aa)
Csal_1975Flagellar basal body FlaE. (387 aa)
Csal_1976Flagellar hook capping protein; Required for flagellar hook formation. May act as a scaffolding protein. (235 aa)
Csal_1977Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. (135 aa)
Csal_1978Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (139 aa)
Csal_1979Flagellar protein FlgA. (251 aa)
Csal_1980Anti-sigma-28 factor, FlgM. (118 aa)
Csal_1981FlgN. (150 aa)
Csal_1985Flagellin-like protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (356 aa)
Csal_1989Methyl-accepting chemotaxis sensory transducer. (556 aa)
fliARNA polymerase, sigma 28 subunit, SigD/FliA/WhiG; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes; Belongs to the sigma-70 factor family. FliA subfamily. (232 aa)
Csal_2014GTP-binding signal recognition particle SRP54, G-protein. (729 aa)
flhAFlagellar biosynthesis protein 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. (695 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. (387 aa)
Csal_2017Chemotaxis phosphatase, CheZ; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). (229 aa)
Csal_2018Response regulator receiver domain protein (CheY-like). (129 aa)
Csal_2019Methyl-accepting chemotaxis sensory transducer. (567 aa)
cheBResponse regulator receiver (CheY-like) modulated CheB methylesterase; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. (354 aa)
Csal_2021MCP methyltransferase, CheR-type; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (290 aa)
Csal_2022Methyl-accepting chemotaxis sensory transducer with Pas/Pac sensor. (748 aa)
Csal_2023CheW protein. (164 aa)
Csal_2024CheA signal transduction histidine kinase. (715 aa)
Csal_2025OmpA/MotB. (330 aa)
Csal_2026Chemotaxis MotA protein. (293 aa)
flhCFlagellar transcriptional activator FlhC; Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways; Belongs to the FlhC family. (203 aa)
flhDPutative flagellar transcriptional activator transcription regulator protein; Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways; Belongs to the FlhD family. (109 aa)
Csal_2029Similar to the cytoplasmic domain of flagellar protein FhlB-like protein. (101 aa)
Csal_2030Hypothetical protein. (406 aa)
Csal_2031Hypothetical protein. (127 aa)
Csal_2032Flagellar protein FliS. (132 aa)
Csal_2033Flagellar hook-associated 2-like 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. (458 aa)
Csal_2778Methyl-accepting chemotaxis sensory transducer. (544 aa)
Your Current Organism:
Chromohalobacter salexigens
NCBI taxonomy Id: 290398
Other names: C. salexigens DSM 3043, Chromohalobacter salexigens 1H11, Chromohalobacter salexigens DSM 3043
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