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AMA52361.1 AMA52361.1 atpB atpB atpE atpE AMA54198.1 AMA54198.1 atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC ppaX ppaX AMA53728.1 AMA53728.1 AMA53718.1 AMA53718.1 AMA53674.1 AMA53674.1 AMA53673.1 AMA53673.1 AMA53590.1 AMA53590.1 AMA53589.1 AMA53589.1 sdhC sdhC sdhA sdhA sdhB sdhB qcrA qcrA qcrB qcrB AMA52769.1 AMA52769.1 AMA52374.1 AMA52374.1 AMA52373.1 AMA52373.1 rbfA rbfA AMA52256.1 AMA52256.1 ctaF ctaF AMA52182.1 AMA52182.1 AMA52181.1 AMA52181.1 AMA52180.1 AMA52180.1 ctaB-2 ctaB-2 ctaA ctaA AMA51916.1 AMA51916.1 ctaB ctaB AMA51734.1 AMA51734.1 AMA51039.1 AMA51039.1 AMA50909.1 AMA50909.1 AMA50908.1 AMA50908.1 ppaC ppaC AMA54383.1 AMA54383.1 AMA54382.1 AMA54382.1 AMA54323.1 AMA54323.1 qoxB qoxB qoxC qoxC qoxD qoxD albF albF albE albE
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:
AMA52361.1Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M16 family. (409 aa)
atpBATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (244 aa)
atpEATP synthase F0F1 subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (70 aa)
AMA54198.1ATP synthase F0F1 subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). Belongs to the ATPase B chain family. (170 aa)
atpHATP synthase F0F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (181 aa)
atpAATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (502 aa)
atpGATP synthase F0F1 subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (287 aa)
atpDATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (473 aa)
atpCATP synthase F0F1 subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (132 aa)
ppaXPyrophosphatase; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool. (216 aa)
AMA53728.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (355 aa)
AMA53718.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (406 aa)
AMA53674.1Subunit D of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; contains an oxidoreductase domain; catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (493 aa)
AMA53673.1Subunit C of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; Derived by automated computational analysis using gene prediction method: Protein Homology. (113 aa)
AMA53590.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (346 aa)
AMA53589.1Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (443 aa)
sdhCSuccinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (202 aa)
sdhAPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology. (586 aa)
sdhBPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (253 aa)
qcrAMenaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (167 aa)
qcrBCytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (224 aa)
AMA52769.1Cytochrome C oxidase Cbb3; Component of the menaquinol-cytochrome c reductase complex. (255 aa)
AMA52374.1Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology. (428 aa)
AMA52373.1Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology. (426 aa)
rbfARibosome-binding factor A; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. (117 aa)
AMA52256.1ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. (890 aa)
ctaFCytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. (110 aa)
AMA52182.1Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (207 aa)
AMA52181.1Cytochrome ubiquinol oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (622 aa)
AMA52180.1Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (356 aa)
ctaB-2Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (305 aa)
ctaAHeme A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 1 subfamily. (306 aa)
AMA51916.1Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (392 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (320 aa)
AMA51734.1(2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (509 aa)
AMA51039.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (300 aa)
AMA50909.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0753 family. (871 aa)
AMA50908.1NADH dehydrogenase; Catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (505 aa)
ppaCInorganic pyrophosphatase; Catalyzes the hydrolysis of pyrophosphate to phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology. (309 aa)
AMA54383.1Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (468 aa)
AMA54382.1Cytochrome d ubiquinol oxidase subunit 2; Derived by automated computational analysis using gene prediction method: Protein Homology. (338 aa)
AMA54323.1Cytochrome ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. (318 aa)
qoxBCytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (649 aa)
qoxCCytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (204 aa)
qoxDQuinol oxidase subunit 4; Derived by automated computational analysis using gene prediction method: Protein Homology. (124 aa)
albFPeptidase M16; Required for production of the bacteriocin subtilosin. Could catalyze some step in the processing of presubtilosin (By similarity). Belongs to the peptidase M16 family. (426 aa)
albEHydrolase; Involved in the production of the bacteriocin subtilosin. (394 aa)
Your Current Organism:
Bacillus subtilis inaquosorum
NCBI taxonomy Id: 483913
Other names: B. subtilis subsp. inaquosorum, BGSC 3A28, Bacillus subtilis subsp. inaquosorum, Bacillus subtilis subsp. inaquosorum Rooney et al. 2009, DSM 22148, KCTC 13429, NRRL B-23052
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