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psaC psaC ndhJ ndhJ ndhK ndhK ndhC ndhC psbE psbE psbF psbF psbL psbL psbJ psbJ ftsH ftsH CB0101_10065 CB0101_10065 psbH psbH psbN psbN psbI psbI CB0101_09730 CB0101_09730 psbK psbK CB0101_10345 CB0101_10345 psbB psbB psaB psaB psaA psaA psaL psaL secY secY ndhN ndhN psbU psbU ndhO ndhO psaE psaE psbV psbV CB0101_06615 CB0101_06615 atpD atpD atpC atpC atpG atpG atpA atpA atpH atpH atpF atpF atpG-2 atpG-2 atpE atpE atpB atpB CB0101_06875 CB0101_06875 CB0101_06880 CB0101_06880 apcB apcB CB0101_06890 CB0101_06890 ccsB ccsB ftsH-2 ftsH-2 psbD psbD psbC psbC CB0101_00495 CB0101_00495 psbA psbA CB0101_00215 CB0101_00215 ndhL ndhL CB0101_00055 CB0101_00055 CB0101_01000 CB0101_01000 CB0101_00915 CB0101_00915 hflB hflB CB0101_01865 CB0101_01865 psaK psaK thf1 thf1 CB0101_02085 CB0101_02085 CB0101_02075 CB0101_02075 CB0101_02965 CB0101_02965 CB0101_02865 CB0101_02865 psb28 psb28 CB0101_03350 CB0101_03350 ccsB-2 ccsB-2 petJ petJ CB0101_03825 CB0101_03825 psbA-2 psbA-2 psb27 psb27 psbQ psbQ secE secE ycf3 ycf3 ndhM ndhM ndhD ndhD nuoK nuoK ndhI ndhI nuoH nuoH ndhH ndhH petD petD petB petB CB0101_14510 CB0101_14510 GCA_000179235_02483 GCA_000179235_02483 CB0101_14270 CB0101_14270 psbX psbX psaJ psaJ petC petC petA petA ndhB ndhB CB0101_12860 CB0101_12860 petG petG ycf4 ycf4 secA secA
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proteins of unknown 3D structure
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psaCUnannotated protein; Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX [...] (102 aa)
ndhJUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (184 aa)
ndhKUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (250 aa)
ndhCUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (120 aa)
psbEUnannotated protein; This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. Belongs to the PsbE/PsbF family. (82 aa)
psbFUnannotated protein; This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. Belongs to the PsbE/PsbF family. (45 aa)
psbLUnannotated protein; One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization. (39 aa)
psbJUnannotated protein; One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. (66 aa)
ftsHUnannotated protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (614 aa)
CB0101_10065Unannotated protein. (273 aa)
psbHUnannotated protein; One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. (66 aa)
psbNUnannotated protein; May play a role in photosystem I and II biogenesis. Belongs to the PsbN family. (39 aa)
psbIUnannotated protein; One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. (39 aa)
CB0101_09730Unannotated protein. (95 aa)
psbKUnannotated protein; One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. (47 aa)
CB0101_10345Unannotated protein; Belongs to the phycobilisome linker protein family. (248 aa)
psbBUnannotated protein; One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation; Belongs to the PsbB/PsbC family. PsbB subfamily. (519 aa)
psaBUnannotated protein; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6; Belongs to the PsaA/PsaB family. (736 aa)
psaAUnannotated protein; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6; Belongs to the PsaA/PsaB family. (767 aa)
psaLUnannotated protein. (163 aa)
secYUnannotated protein; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. (438 aa)
ndhNUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (155 aa)
psbUUnannotated protein; Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation. (125 aa)
ndhOUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (81 aa)
psaEUnannotated protein; Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase; Belongs to the PsaE family. (69 aa)
psbVUnannotated protein; Low-potential cytochrome c that plays a role in the oxygen- evolving complex of photosystem II. (169 aa)
CB0101_06615Unannotated protein. (263 aa)
atpDUnannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (486 aa)
atpCUnannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. (134 aa)
atpGUnannotated protein; 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. (317 aa)
atpAUnannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (505 aa)
atpHUnannotated protein; 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)
atpFUnannotated protein; 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. (172 aa)
atpG-2Unannotated protein; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. Belongs to the ATPase B chain family. (153 aa)
atpEUnannotated protein; 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. (82 aa)
atpBUnannotated protein; 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. (242 aa)
CB0101_06875Unannotated protein; Belongs to the phycobilisome linker protein family. (1008 aa)
CB0101_06880Unannotated protein. (161 aa)
apcBUnannotated protein. (162 aa)
CB0101_06890Unannotated protein; Rod linker protein, associated with allophycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. (66 aa)
ccsBUnannotated protein; Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. (431 aa)
ftsH-2Unannotated protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (626 aa)
psbDUnannotated protein; Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex. (135 aa)
psbCUnannotated protein; One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation; Belongs to the PsbB/PsbC family. PsbC subfamily. (462 aa)
CB0101_00495Unannotated protein. (172 aa)
psbAUnannotated protein; Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. (359 aa)
CB0101_00215Unannotated protein. (358 aa)
ndhLUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (83 aa)
CB0101_00055Unannotated protein. (128 aa)
CB0101_01000Unannotated protein; Belongs to the phycobilisome linker protein family. (354 aa)
CB0101_00915Unannotated protein. (211 aa)
hflBUnannotated protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (600 aa)
CB0101_01865Unannotated protein. (189 aa)
psaKUnannotated protein. (85 aa)
thf1Unannotated protein; May be involved in photosynthetic membrane biogenesis. (224 aa)
CB0101_02085Unannotated protein; Belongs to the orange carotenoid-binding protein family. (317 aa)
CB0101_02075Unannotated protein. (109 aa)
CB0101_02965Unannotated protein. (227 aa)
CB0101_02865Unannotated protein. (164 aa)
psb28Unannotated protein; Belongs to the Psb28 family. (123 aa)
CB0101_03350Unannotated protein. (176 aa)
ccsB-2Unannotated protein; Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. (306 aa)
petJUnannotated protein; Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. (113 aa)
CB0101_03825Unannotated protein. (540 aa)
psbA-2Unannotated protein; Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. (358 aa)
psb27Unannotated protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster. (135 aa)
psbQUnannotated protein. (163 aa)
secEUnannotated protein; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. (80 aa)
ycf3Unannotated protein; Seems to be required for the assembly of the photosystem I complex; Belongs to the Ycf3 family. (182 aa)
ndhMUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (115 aa)
ndhDUnannotated protein; NDH-1 shuttles electrons from NAD(P)H, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4 family. (543 aa)
nuoKUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (109 aa)
ndhIUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (200 aa)
nuoHUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (380 aa)
ndhHUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (394 aa)
petDUnannotated protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. (160 aa)
petBUnannotated protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. (226 aa)
CB0101_14510Unannotated protein; Belongs to the peptidase S41A family. (407 aa)
GCA_000179235_02483Unannotated protein. (135 aa)
CB0101_14270Unannotated protein; Belongs to the phycobilisome linker protein family. (252 aa)
psbXUnannotated protein; Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II. (40 aa)
psaJUnannotated protein; May help in the organization of the PsaE and PsaF subunits. Belongs to the PsaJ family. (38 aa)
petCUnannotated protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. (182 aa)
petAUnannotated protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. (310 aa)
ndhBUnannotated protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (509 aa)
CB0101_12860Unannotated protein. (394 aa)
petGUnannotated protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex. (37 aa)
ycf4Unannotated protein; Seems to be required for the assembly of the photosystem I complex; Belongs to the Ycf4 family. (188 aa)
secAUnannotated protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family. (956 aa)
Your Current Organism:
Synechococcus sp. CB0101
NCBI taxonomy Id: 232348
Other names: S. sp. CB0101
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