CC_0674 protein (Caulobacter vibrioides CB15)

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CC_0674

Hypothetical protein; Identified by Glimmer2; putative. (389 aa)

Predicted Functional Partners:

CC_1947

0.771

CC_1946

0.750

CC_0454

0.709

nuoD

0.708

nuoI

0.689

CC_1800

0.681

nuoC

0.662

nuoH

0.626

CC_1950

0.588

CC_2925

0.553

Your Current Organism:

Caulobacter vibrioides CB15

NCBI taxonomy Id: 190650
Other names: C. vibrioides CB15, Caulobacter crescentus CB15, Caulobacter vibrioides ATCC 19089

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CC_0454	CC_0674	CC_0454	CC_0674	TonB-dependent receptor; Similar to GP:9948370; identified by sequence similarity; putative.	Hypothetical protein; Identified by Glimmer2; putative.	0.709
CC_0454	CC_2925	CC_0454	CC_2925	TonB-dependent receptor; Similar to GP:9948370; identified by sequence similarity; putative.	Hypothetical protein; Identified by Glimmer2; putative.	0.422
CC_0674	CC_0454	CC_0674	CC_0454	Hypothetical protein; Identified by Glimmer2; putative.	TonB-dependent receptor; Similar to GP:9948370; identified by sequence similarity; putative.	0.709
CC_0674	CC_1800	CC_0674	CC_1800	Hypothetical protein; Identified by Glimmer2; putative.	Hypothetical protein; Identified by Glimmer2; putative.	0.681
CC_0674	CC_1946	CC_0674	CC_1946	Hypothetical protein; Identified by Glimmer2; putative.	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	0.750
CC_0674	CC_1947	CC_0674	CC_1947	Hypothetical protein; Identified by Glimmer2; putative.	NADH dehydrogenase I, F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.	0.771
CC_0674	CC_1950	CC_0674	CC_1950	Hypothetical protein; Identified by Glimmer2; putative.	NADH dehydrogenase I, E subunit; Identified by match to PFAM protein family HMM PF01257.	0.588
CC_0674	CC_2925	CC_0674	CC_2925	Hypothetical protein; Identified by Glimmer2; putative.	Hypothetical protein; Identified by Glimmer2; putative.	0.553
CC_0674	nuoC	CC_0674	CC_1954	Hypothetical protein; Identified by Glimmer2; putative.	NADH dehydrogenase I, C subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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 30 kDa subunit family.	0.662
CC_0674	nuoD	CC_0674	CC_1952	Hypothetical protein; Identified by Glimmer2; putative.	NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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 49 kDa subunit family.	0.708
CC_0674	nuoH	CC_0674	CC_1945	Hypothetical protein; Identified by Glimmer2; putative.	NADH dehydrogenase I, H subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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. This subunit may bind ubiquinone.	0.626
CC_0674	nuoI	CC_0674	CC_1942	Hypothetical protein; Identified by Glimmer2; putative.	NADH dehydrogenase I, I subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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.	0.689
CC_1800	CC_0674	CC_1800	CC_0674	Hypothetical protein; Identified by Glimmer2; putative.	Hypothetical protein; Identified by Glimmer2; putative.	0.681
CC_1946	CC_0674	CC_1946	CC_0674	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	Hypothetical protein; Identified by Glimmer2; putative.	0.750
CC_1946	CC_1947	CC_1946	CC_1947	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	NADH dehydrogenase I, F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.	0.999
CC_1946	CC_1950	CC_1946	CC_1950	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	NADH dehydrogenase I, E subunit; Identified by match to PFAM protein family HMM PF01257.	0.999
CC_1946	nuoC	CC_1946	CC_1954	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	NADH dehydrogenase I, C subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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 30 kDa subunit family.	0.999
CC_1946	nuoD	CC_1946	CC_1952	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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 49 kDa subunit family.	0.999
CC_1946	nuoH	CC_1946	CC_1945	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	NADH dehydrogenase I, H subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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. This subunit may bind ubiquinone.	0.999
CC_1946	nuoI	CC_1946	CC_1942	NADH dehydrogenase I, G subunit; 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 75 kDa subunit family.	NADH dehydrogenase I, I subunit; NDH-1 shuttles electrons from NADH, 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 ubiquinone. 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.	0.999