LHA_0809 protein (Legionella hackeliae) - STRING interaction network

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LHA_0809

Protein-L-isoaspartate-O-methyltransferase. (217 aa)

Predicted Functional Partners:

LHA_1498

0.899

tolC

0.879

coxB

0.867

nuoG

0.865

nuoC

0.840

nuoA

0.820

nuoD

0.791

ttcA

0.716

kbl

0.707

nuoN

0.682

Your Current Organism:

Legionella hackeliae

NCBI taxonomy Id: 449
Other names: ATCC 35250, CCUG 31232, CCUG 31232 A, CIP 103844, DSM 19214, JCM 7563, L. hackeliae, NCTC 11979, strain Lansing 2

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
LHA_0809	LHA_1498	LHA_0809	LHA_1498	Protein-L-isoaspartate-O-methyltransferase.	Putative erythromycin esterase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.899
LHA_0809	coxB	LHA_0809	LHA_0116	Protein-L-isoaspartate-O-methyltransferase.	Cytochrome c oxidase subunit 2; 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).	0.867
LHA_0809	kbl	LHA_0809	LHA_0810	Protein-L-isoaspartate-O-methyltransferase.	2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.	0.707
LHA_0809	nuoA	LHA_0809	LHA_2994	Protein-L-isoaspartate-O-methyltransferase.	NADH-quinone oxidoreductase subunit A; 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 subunit 3 family.	0.820
LHA_0809	nuoC	LHA_0809	LHA_2992	Protein-L-isoaspartate-O-methyltransferase.	NADH-quinone oxidoreductase subunit C; 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.	0.840
LHA_0809	nuoD	LHA_0809	LHA_2991	Protein-L-isoaspartate-O-methyltransferase.	NADH-quinone oxidoreductase subunit D; 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.	0.791
LHA_0809	nuoG	LHA_0809	LHA_2988	Protein-L-isoaspartate-O-methyltransferase.	NADH-quinone oxidoreductase; 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.	0.865
LHA_0809	nuoN	LHA_0809	LHA_2981	Protein-L-isoaspartate-O-methyltransferase.	NADH-quinone oxidoreductase subunit N; 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 subunit 2 family.	0.682
LHA_0809	tolC	LHA_0809	LHA_0808	Protein-L-isoaspartate-O-methyltransferase.	Outer membrane protein TolC.	0.879
LHA_0809	ttcA	LHA_0809	LHA_0807	Protein-L-isoaspartate-O-methyltransferase.	tRNA 2-thiocytidine biosynthesis protein TtcA; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.	0.716
LHA_1498	LHA_0809	LHA_1498	LHA_0809	Putative erythromycin esterase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Protein-L-isoaspartate-O-methyltransferase.	0.899
coxB	LHA_0809	LHA_0116	LHA_0809	Cytochrome c oxidase subunit 2; 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).	Protein-L-isoaspartate-O-methyltransferase.	0.867
coxB	nuoA	LHA_0116	LHA_2994	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase subunit A; 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 subunit 3 family.	0.990
coxB	nuoC	LHA_0116	LHA_2992	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase subunit C; 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.	0.976
coxB	nuoD	LHA_0116	LHA_2991	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase subunit D; 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.	0.946
coxB	nuoG	LHA_0116	LHA_2988	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase; 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.	0.933
coxB	nuoN	LHA_0116	LHA_2981	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase subunit N; 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 subunit 2 family.	0.990
kbl	LHA_0809	LHA_0810	LHA_0809	2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.	Protein-L-isoaspartate-O-methyltransferase.	0.707
kbl	tolC	LHA_0810	LHA_0808	2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.	Outer membrane protein TolC.	0.704
kbl	ttcA	LHA_0810	LHA_0807	2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.	tRNA 2-thiocytidine biosynthesis protein TtcA; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.	0.620