NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
At least 10 million metric tons of volatile dimethyl sulfide (DMS) are released into the atmosphere annually by the dimethylsulfonioproprionate lyase in oceans. It is a component of the tangy aroma of the seaside and functions as a chemical attractant that guides various marine animals, such as sea birds, invertebrates, and some mammals, toward potential food supplies. DMS oxidation products act as condensation nuclei, causing water molecules to coalesce, with possible effects on local climate through enhanced cloud formation.
Belongs to the aspartate/glutamate racemases family. ALMA1 subfamily.
Protein Spotlight; The smell of the sea - Issue 174 of December 2015
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle. Constitutes by far the most highly expressed Alma gene in CCMP373 strain.
Decreases dimethylsulfonioproprionate lyase activity by a factor of 75.
Abolishes dimethylsulfonioproprionate lyase activity.
ATP synthase alpha/beta chain, C-terminal domain
P-loop containing nucleotide triphosphate hydrolases
ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
C-terminal domain of alpha and beta subunits of F1 ATP synthase
N-terminal domain of alpha and beta subunits of F1 ATP synthase
P-loop containing nucleoside triphosphate hydrolases
ATP synthase subunit alpha, chloroplastic
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c.
Belongs to the ATPase alpha/beta chains family.
ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
ATP synthase subunit beta, chloroplastic
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12).
N-terminal domain of the delta subunit of the F1F0-ATP synthase
ATP SYNTHASE SUBUNIT DELTA, CHLOROPLASTIC
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.
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.
Belongs to the ATPase delta chain family.
F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC
Epsilon subunit of F1F0-ATP synthase N-terminal domain
Produces ATP from ADP in the presence of a proton gradient across the membrane.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Belongs to the ATPase epsilon chain family.
F1F0 ATP synthase subunit B, membrane domain
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.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.
In plastids the F-type ATPase is also known as CF(1)CF(0).
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Plastid genome size and heterogeneous base composition of nuclear DNA from Ochrosphaera neapolitana (Prymnesiophyta).
ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Reversibly protonated during proton transport
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c (By similarity).
CYTOCHROME C BIOGENESIS PROTEIN CCS1, CHLOROPLASTIC
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
TCP-1-like chaperonin intermediate domain
60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Belongs to the chaperonin (HSP60) family.
Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Binds 1 heme c group covalently per subunit.
Part of the oxygen-evolving complex of photosystem II.
Associated with photosystem II at the lumenal side of the thylakoid membrane.
Belongs to the cytochrome c family. PsbV subfamily.
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.
Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently.
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer.
Heme 1 (or BH or b566) is high-potential and absorbs at about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs at about 562 nm.
Belongs to the cytochrome b family. PetB subfamily.
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
50% of the molecules were found to be monomethylated at Lys-24.
Belongs to the cytochrome c family. PetJ subfamily.
Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer (By similarity).
Cytochrome b5-like heme/steroid binding domain
Fatty acid desaturase that introduces a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta(7) double bond, resulting in the production of delta-4 desaturated fatty acid docosahexanoic acid (DHA). Mediates desaturation of 22:5n-3 and 22:4n-6 into 22:6n-3 and 22:5n-6 respectively.
The cytochrome b5 heme-binding domain acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
Belongs to the fatty acid desaturase type 1 family.
Fatty acid desaturase that introduces a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta(7) double bond, resulting in the production of delta-4 desaturated fatty acid docosahexanoic acid (DHA).
Fatty acid desaturase that introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond.
Fatty acid desaturase that introduces a cis double bond at the 8-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond to yield (20:4(8,11,14,17)).
Heat shock protein 70kD (HSP70), peptide-binding domain
Belongs to the heat shock protein 70 family.
Heat shock protein 70kD (HSP70), C-terminal subdomain
EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN 3.2, CHLOROPLASTIC
Fucoxanthin-chlorophyll a-c binding protein, chloroplastic
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Energy is transferred from the carotenoid and chlorophyll C (or B) to chlorophyll A and the photosynthetic reaction centers where it is used to synthesize ATP and reducing power.
The LHC complex of chromophytic algae is composed of fucoxanthin, chlorophyll A and C bound non-covalently by fucoxanthin chlorophyll proteins (FCPs). The ratio of pigments in this LHC is; fucoxanthin: chlorophyll C: chlorophyll A; (0.6-1): (0.1-0.3): (1).
FCPs are probably transported across the endoplasmic reticulum membranes that surround the plastid via a signal peptide, followed by translocation across the thylakoid membrane via a transit peptide.
Expression is increased 5-fold under conditions of low light.
Belongs to the fucoxanthin chlorophyll protein family.
Plays a key role in the nitrogen metabolism of microorganisms, animals and plants.
Belongs to the glutamine synthetase family.
SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED
Putative septum site-determining protein MinD
ATPase required for the correct placement of the division site.
Belongs to the ParA family. MinD subfamily.
a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Belongs to the cytochrome b family. PetD subfamily.
PetG subunit of the cytochrome b6f complex
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.
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. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
PetM subunit of the cytochrome b6f complex
PetN subunit of the cytochrome b6f complex
PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2
Photosystem I P700 chlorophyll a apoprotein A1
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.
P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits.
PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED
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, FA and FB in turn.
Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
The eukaryotic PSI reaction center is composed of at least 11 subunits.
Subunit VIII of photosystem I reaction centre, PsaI
Photosystem I reaction center subunit VIII
May help in the organization of the PsaL subunit.
PHOTOSYSTEM I REACTION CENTER SUBUNIT IX
Subunit IX of photosystem I reaction centre, PsaJ
May help in the organization of the PsaE and PsaF subunits.
Photosystem I PsaL, reaction centre subunit XI
PHOTOSYSTEM I REACTION CENTER SUBUNIT XI, CHLOROPLASTIC
Photosystem I reaction center subunit XI, PsaL
Photosystem I reaction center subunit XI
Subunit XII of photosystem I reaction centre, PsaM
Photosystem I reaction center subunit XII
Bacterial photosystem II reaction centre, L and M subunits
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.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.
2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.
Belongs to the reaction center PufL/M/PsbA/D family.
ligand shared with heterodimeric partner
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.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Photosystem II cytochrome b559, alpha subunit
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.
With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Heterodimer of an alpha subunit and a beta subunit. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Photosystem II reaction center protein H
Photosystem II 10 kDa phosphoprotein PsbH
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.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, numerous small proteins, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
PHOTOSYSTEM II REACTION CENTER PROTEIN I
Photosystem II reaction center protein I, PsbI
Photosystem II reaction center protein J, PsbJ
Photosystem II reaction center protein J
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.
PHOTOSYSTEM II REACTION CENTER PROTEIN K
Photosystem II reaction center protein K, PsbK
Photosystem II reaction center protein L, PsbL
Photosystem II reaction center protein L
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.
May play a role in photosystem I and II biogenesis.
Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true.
PHOTOSYSTEM II REACTION CENTER PROTEIN T
Photosystem II reaction center protein T, PsbT
Seems to play a role in the dimerization of PSII.
Photosystem II reaction center X protein
Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
PSII consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. PSII forms dimeric complexes.
Belongs to the PsbX family. Type 1 subfamily.
Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
PHOTOSYSTEM II REACTION CENTER PROTEIN Z
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Associated with the photosystem II complex.
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Probable RuBisCO transcriptional regulator
Trans-acting transcriptional regulator of RuBisCO genes (rbcL and rbcS) expression.
Belongs to the LysR transcriptional regulatory family.
Ribulose bisphosphate carboxylase, large subunit, C-terminal domain
RuBisCO large subunit, N-terminal domain
RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
RuBisCO, large subunit, small (N-terminal) domain
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity).
Heterohexadecamer of 8 large chains and 8 small chains.
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel' (By similarity).
Belongs to the RuBisCO large chain family. Type I subfamily.
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.
Ribulose bisphosphate carboxylase, small subunit
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Heterohexadecamer of 8 large and 8 small subunits.
In this alga, in contrast to plants, the small subunit is encoded in the chloroplast.
Belongs to the RuBisCO small chain family.
54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL
50S ribosomal protein L14, chloroplastic
Belongs to the universal ribosomal protein uL14 family.
39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL
50S ribosomal protein L16, chloroplastic
Belongs to the universal ribosomal protein uL16 family.
50S RIBOSOMAL PROTEIN L20, CHLOROPLASTIC
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Belongs to the bacterial ribosomal protein bL20 family.
39S RIBOSOMAL PROTEIN L21, MITOCHONDRIAL
50S ribosomal protein L21, chloroplastic
Belongs to the bacterial ribosomal protein bL21 family.
50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC
CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED
This protein binds specifically to 23S rRNA.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Belongs to the universal ribosomal protein uL22 family.
RIBOSOMAL_L23EN DOMAIN-CONTAINING PROTEIN
50S ribosomal protein L23, chloroplastic
Belongs to the universal ribosomal protein uL23 family.
39S RIBOSOMAL PROTEIN L27, MITOCHONDRIAL
50S ribosomal protein L27, chloroplastic
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the universal ribosomal protein uL2 family.
50S RIBOSOMAL PROTEIN L31, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
50S RIBOSOMAL PROTEIN L33, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL33 family.
50S ribosomal protein L34, chloroplastic
Belongs to the bacterial ribosomal protein bL34 family.
50S ribosomal protein L36, chloroplastic
Belongs to the bacterial ribosomal protein bL36 family.
50S RIBOSOMAL PROTEIN L3-1, CHLOROPLASTIC
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the universal ribosomal protein uL3 family.
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
Part of the 50S ribosomal subunit; contacts the 5S rRNA.
Belongs to the universal ribosomal protein uL5 family.
Belongs to the universal ribosomal protein uL6 family.
5' to 3' exonuclease, C-terminal subdomain
DNA-directed RNA polymerase, insert domain
C-terminal domain of RNA polymerase alpha subunit
Insert subdomain of RNA polymerase alpha subunit
DNA-directed RNA polymerase subunit alpha
Plastid-encoded RNA polymerase subunit alpha
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Belongs to the RNA polymerase alpha chain family.
DNA-directed RNA polymerase, beta subunit, external 1 domain
DNA-directed RNA polymerase, subunit 2, domain 6
RNA polymerase alpha subunit dimerisation domain
DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA
beta and beta-prime subunits of DNA dependent RNA-polymerase
Plastid-encoded RNA polymerase subunit beta
Belongs to the RNA polymerase beta chain family.
DNA-directed RNA polymerase subunit beta'
Plastid-encoded RNA polymerase subunit beta'
Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.
DNA-directed RNA polymerase subunit beta''
Plastid-encoded RNA polymerase subunit beta''
Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
37S RIBOSOMAL PROTEIN S10, MITOCHONDRIAL
30S ribosomal protein S10, chloroplastic
Involved in the binding of tRNA to the ribosomes.
Belongs to the universal ribosomal protein uS10 family.
28S RIBOSOMAL PROTEIN S11, MITOCHONDRIAL
40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
30S ribosomal protein S11, chloroplastic
Belongs to the universal ribosomal protein uS11 family.
28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL
30S ribosomal protein S12, chloroplastic
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity).
Belongs to the universal ribosomal protein uS12 family.
30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18
37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL
30S ribosomal protein S13, chloroplastic
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.
Belongs to the universal ribosomal protein uS13 family.
28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL
Glucocorticoid receptor-like (DNA-binding domain)
30S ribosomal protein S14, chloroplastic
Binds 16S rRNA, required for the assembly of 30S particles.
Belongs to the universal ribosomal protein uS14 family.
28S RIBOSOMAL PROTEIN S16, MITOCHONDRIAL
30S ribosomal protein S16, chloroplastic
Belongs to the bacterial ribosomal protein bS16 family.
37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL
30S ribosomal protein S17, chloroplastic
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS17 family.
28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL
30S ribosomal protein S18, chloroplastic
Belongs to the bacterial ribosomal protein bS18 family.
37S RIBOSOMAL PROTEIN S19, MITOCHONDRIAL
30S ribosomal protein S19, chloroplastic
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS19 family.
30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR
Belongs to the universal ribosomal protein uS2 family.
Prokaryotic type KH domain (KH-domain type II)
Belongs to the universal ribosomal protein uS3 family.
37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
With S5 and S12 plays an important role in translational accuracy.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity (By similarity).
Belongs to the universal ribosomal protein uS4 family.
With S4 and S12 plays an important role in translational accuracy.
Part of the 30S ribosomal subunit. Contacts protein S4 (By similarity).
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Belongs to the universal ribosomal protein uS5 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Belongs to the universal ribosomal protein uS7 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Belongs to the universal ribosomal protein uS8 family.
Belongs to the universal ribosomal protein uS9 family.
Helical scaffold and wing domains of SecA
SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM
Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
A minor fraction is associated with the chloroplast thylakoid membrane.
PREPROTEIN TRANSLOCASE SUBUNIT SCY2, CHLOROPLASTIC
The central subunit of the protein translocation channel SecYE. 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.
Component of the plastid Sec protein translocase complex, which is composed of at least SecY and SecE.
The central subunit of the protein translocation channel SecYE. 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 (By similarity).
Component of the plastid Sec protein translocase complex, which is composed of at least SecY, SecE and SecG.
PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED
Protein disulfide-isomerase-like protein EhSep2
Belongs to the protein disulfide isomerase family.
Contains a selenocysteine rather than a cysteine at one of the conserved active site positions so does not form the disulfide bond normally required for protein disulfide isomerase activity.
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Homotetramer. Forms heterodimers with either ThiH or ThiS.
FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Activity was very low in selenium-depleted cells, but increased 4-fold to the same level as in selenium-sufficient cells for 70 hours after the addition of 10 nm selenite.
The thioredoxin reductase active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
A gene encoding the 16 kD proteolipid subunit of a vacuolar-type H(+)-ATPase from Pleurochrysis carterae strain 136.
V-TYPE PROTON ATPASE 16 KDA PROTEOLIPID SUBUNIT
V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT
Vacuolar proton pump 16 kDa proteolipid subunit
Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein; which is present as a hexamer that forms the proton-conducting pore).
Belongs to the V-ATPase proteolipid subunit family.
Photosystem II reaction center protein Ycf12
A core subunit of photosystem II (PSII).
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Seems to be required for the assembly of the photosystem I complex.
Uncharacterized 10.9 kDa protein in secA 5'region
Uncharacterized 4.8 kDa protein in secA 3'region