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atpC atpC atpG atpG atpA atpA atpH atpH atpD atpD
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:
atpCATP synthase F0F1 subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (153 aa)
atpGATP synthase 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. (320 aa)
atpAATP F0F1 synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (503 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. (182 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. (479 aa)
Your Current Organism:
Lactobacillus helveticus
NCBI taxonomy Id: 1587
Other names: ATCC 15009, Bacillus casei e, Bacillus e, CCUG 30139, CIP 103146, Caseobacterium e, DSM 20075, IFO 15019, L. helveticus, LMG 13555, LMG 22464 [[Lactobacillus suntoryeus]], LMG 6413, LMG:13555, LMG:22464 [[Lactobacillus suntoryeus]], LMG:6413, Lactobacillus helveticum, Lactobacillus sp. NCIM 2126, Lactobacillus sp. NCIM 2733, Lactobacillus suntoryeus, Lactobacillus suntoryeus Cachat and Priest 2005, Lactobacterium helveticum, NBRC 15019, NCIMB 14005 [[Lactobacillus suntoryeus]], NRRL B-4526, Plocamobacterium helveticum, Thermobacterium helveticum, strain SA [[Lactobacillus suntoryeus]]
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