STRINGSTRING
rbfA rbfA ppa ppa KJL45086.1 KJL45086.1 KJL44963.1 KJL44963.1 KJL44819.1 KJL44819.1 KJL44446.1 KJL44446.1 atpB atpB atpE atpE atpF atpF atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC ppk ppk sdhA_1 sdhA_1 ctaA ctaA ctaB ctaB ctaE ctaE qcrC qcrC aioB aioB petB petB ctaD ctaD ctaC ctaC yjlD yjlD KJL41824.1 KJL41824.1 ctpF ctpF cydA cydA cydB cydB KJL41623.1 KJL41623.1 yoaB yoaB petC1 petC1 sdhB sdhB sdhA_2 sdhA_2 KJL41175.1 KJL41175.1 KJL41176.1 KJL41176.1 KJL40211.1 KJL40211.1 mrpC mrpC mrpD mrpD
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:
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. (144 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (177 aa)
KJL45086.1Polyphosphate kinase 2 (PPK2). (301 aa)
KJL44963.1Polyphosphate kinase 2 (PPK2). (287 aa)
KJL44819.1NADH dehydrogenase-like protein. (484 aa)
KJL44446.1Polyphosphate kinase 2 (PPK2). (272 aa)
atpBATP synthase subunit a. (239 aa)
atpEATP synthase 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. (78 aa)
atpFATP synthase 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. (185 aa)
atpHATP synthase 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. (263 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. (545 aa)
atpGATP synthase gamma chain; 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. (298 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. (482 aa)
atpCATP synthase epsilon chain. (86 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. (736 aa)
sdhA_1Succinate dehydrogenase flavoprotein subunit. (593 aa)
ctaAHeme A synthase. (318 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. (313 aa)
ctaECytochrome c oxidase subunit 3. (213 aa)
qcrCMenaquinol-cytochrome c reductase cytochrome c subunit. (267 aa)
aioBArsenite oxidase subunit AioB precursor. (359 aa)
petBCytochrome b6. (616 aa)
ctaDCytochrome c oxidase subunit 1; 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. (587 aa)
ctaCCytochrome c oxidase subunit 2 precursor. (298 aa)
yjlDNADH dehydrogenase-like protein YjlD. (403 aa)
KJL41824.1Nucleotidyltransferase domain protein. (260 aa)
ctpFPutative cation-transporting ATPase F. (923 aa)
cydACytochrome bd ubiquinol oxidase subunit 1. (481 aa)
cydBCytochrome bd-I ubiquinol oxidase subunit 2. (344 aa)
KJL41623.1Polyphosphate kinase 2 (PPK2). (303 aa)
yoaBCalcium-transporting ATPase 1. (906 aa)
petC1Cytochrome b6-f complex iron-sulfur subunit 1. (563 aa)
sdhBSuccinate dehydrogenase iron-sulfur subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (266 aa)
sdhA_2Succinate dehydrogenase flavoprotein subunit. (607 aa)
KJL41175.1Succinate dehydrogenase/Fumarate reductase transmembrane subunit. (149 aa)
KJL41176.1Succinate dehydrogenase/Fumarate reductase transmembrane subunit. (114 aa)
KJL40211.1Putative permease. (362 aa)
mrpCNa(+)/H(+) antiporter subunit C. (181 aa)
mrpDNa(+)/H(+) antiporter subunit D. (527 aa)
Your Current Organism:
Microbacterium trichothecenolyticum
NCBI taxonomy Id: 69370
Other names: ATCC 51475, Aureibacterium trichothecenolyticum, Aureobacterium trichothecenolyticum, CIP 103817, DSM 8608, IFO 15077, LMG 16696, LMG:16696, M. trichothecenolyticum, Microbacterium sp. BDR3P1B1, NBRC 15077
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