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atpE atpE lin1195 lin1195 lin0134 lin0134 atpI atpI atpB atpB atpF atpF
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
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Your Input:
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. (72 aa)
lin1195Endonuclease MutS2; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. (785 aa)
lin0134ATP 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. (80 aa)
atpIAtpI protein; Highly similar to ATP synthase subunit i. (132 aa)
atpBATP synthase subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (238 aa)
atpFATP synthase subunit b; 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. (170 aa)
Your Current Organism:
Listeria innocua
NCBI taxonomy Id: 272626
Other names: L. innocua Clip11262, Listeria innocua Clip11262, Listeria innocua str. Clip11262, Listeria innocua strain Clip11262
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