(60 nodes) Primary active transmembrane transporter activity network (Synechococcus sp. CB0101)

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:
	CB0101_13325	Unannotated protein. (202 aa)
	CB0101_02230	Unannotated protein. (298 aa)
	CB0101_03565	Unannotated protein. (588 aa)
	secD	Unannotated protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. (493 aa)
	secF	Unannotated protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (330 aa)
	CB0101_03970	Unannotated protein. (92 aa)
	CB0101_03825	Unannotated protein. (540 aa)
	CB0101_04475	Unannotated protein. (896 aa)
	CB0101_04385	Unannotated protein. (866 aa)
	CB0101_04340	Unannotated protein. (741 aa)
	CB0101_04255	Unannotated protein. (521 aa)
	CB0101_04965	Unannotated protein; Belongs to the ABC transporter superfamily. (375 aa)
	CB0101_04950	Unannotated protein. (599 aa)
	CB0101_04890	Unannotated protein. (502 aa)
	CB0101_04885	Unannotated protein. (620 aa)
	CB0101_04795	Unannotated protein. (623 aa)
	CB0101_04790	Unannotated protein. (497 aa)
	CB0101_04675	Unannotated protein. (920 aa)
	CB0101_14605	Unannotated protein. (791 aa)
	CB0101_14705	Unannotated protein. (670 aa)
	ndhD	Unannotated 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)
	CB0101_14760	Unannotated protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 6 family. (199 aa)
	ndhI	Unannotated 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)
	CB0101_14140	Unannotated protein. (661 aa)
	cobD	Unannotated protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. (384 aa)
	petC	Unannotated 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)
	CB0101_13315	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (277 aa)
	ctaD	Unannotated protein; 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. (555 aa)
	CB0101_02565	Unannotated protein. (291 aa)
	ndhB	Unannotated 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_12560	Unannotated protein. (596 aa)
	CB0101_12450	Unannotated protein. (651 aa)
	GCA_000179235_02989	Unannotated protein. (160 aa)
	CB0101_08880	Unannotated protein. (982 aa)
	CB0101_08965	Unannotated protein. (416 aa)
	secA	Unannotated 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)
	ndhJ	Unannotated 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)
	ndhK	Unannotated 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)
	ndhC	Unannotated 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)
	CB0101_09385	Unannotated protein. (615 aa)
	CB0101_09380	Unannotated protein. (605 aa)
	CB0101_10885	Unannotated protein. (728 aa)
	CB0101_11690	Unannotated protein; Belongs to the ABC transporter superfamily. (414 aa)
	CB0101_06500	Unannotated protein. (733 aa)
	secG	Unannotated protein; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. (77 aa)
	atpD	Unannotated 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)
	CB0101_06805	Unannotated protein. (147 aa)
	atpA	Unannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (505 aa)
	cobQ	Unannotated protein; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. (500 aa)
	CB0101_00115	Unannotated protein. (201 aa)
	CB0101_00110	Unannotated protein; Belongs to the heme-copper respiratory oxidase family. (562 aa)
	CB0101_00105	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (315 aa)
	GCA_000179235_01199	Unannotated protein. (765 aa)
	CB0101_00585	Unannotated protein. (687 aa)
	CB0101_01035	Unannotated protein. (323 aa)
	CB0101_01030	Unannotated protein. (334 aa)
	pstB	Unannotated protein; Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system; Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family. (274 aa)
	CB0101_01560	Unannotated protein. (513 aa)
	CB0101_01370	Unannotated protein. (578 aa)
	pstB-2	Unannotated protein; Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system; Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family. (264 aa)

Your Current Organism:

Synechococcus sp. CB0101

NCBI taxonomy Id: 232348
Other names: S. sp. CB0101

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CB0101_00105	CB0101_00110	GCA_000179235_01148	GCA_000179235_01147	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein; Belongs to the heme-copper respiratory oxidase family.	0.999
CB0101_00105	CB0101_00115	GCA_000179235_01148	GCA_000179235_01146	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein.	0.999
CB0101_00105	CB0101_03825	GCA_000179235_01148	GCA_000179235_01862	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein.	0.642
CB0101_00105	CB0101_04255	GCA_000179235_01148	GCA_000179235_01979	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein.	0.971
CB0101_00105	CB0101_04790	GCA_000179235_01148	GCA_000179235_02064	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein.	0.642
CB0101_00105	CB0101_04890	GCA_000179235_01148	GCA_000179235_02044	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein.	0.642
CB0101_00105	CB0101_13315	GCA_000179235_01148	GCA_000179235_02715	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.917
CB0101_00105	CB0101_13325	GCA_000179235_01148	GCA_000179235_02717	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein.	0.998
CB0101_00105	ctaD	GCA_000179235_01148	GCA_000179235_02716	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated protein; 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.	0.998
CB0101_00105	ndhB	GCA_000179235_01148	GCA_000179235_02728	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated 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.	0.782
CB0101_00105	ndhC	GCA_000179235_01148	GCA_000179235_00270	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated 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.	0.813
CB0101_00105	ndhD	GCA_000179235_01148	GCA_000179235_02400	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated 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.	0.642
CB0101_00105	ndhJ	GCA_000179235_01148	GCA_000179235_00268	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated 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.	0.733
CB0101_00105	ndhK	GCA_000179235_01148	GCA_000179235_00269	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated 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.	0.622
CB0101_00105	petC	GCA_000179235_01148	GCA_000179235_02693	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Unannotated 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.	0.852
CB0101_00110	CB0101_00105	GCA_000179235_01147	GCA_000179235_01148	Unannotated protein; Belongs to the heme-copper respiratory oxidase family.	Unannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.999
CB0101_00110	CB0101_00115	GCA_000179235_01147	GCA_000179235_01146	Unannotated protein; Belongs to the heme-copper respiratory oxidase family.	Unannotated protein.	0.999
CB0101_00110	CB0101_03825	GCA_000179235_01147	GCA_000179235_01862	Unannotated protein; Belongs to the heme-copper respiratory oxidase family.	Unannotated protein.	0.711
CB0101_00110	CB0101_04255	GCA_000179235_01147	GCA_000179235_01979	Unannotated protein; Belongs to the heme-copper respiratory oxidase family.	Unannotated protein.	0.978
CB0101_00110	CB0101_04790	GCA_000179235_01147	GCA_000179235_02064	Unannotated protein; Belongs to the heme-copper respiratory oxidase family.	Unannotated protein.	0.714