lolD protein (Proteus vulgaris) - STRING interaction network

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lolD

Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. (228 aa)

Predicted Functional Partners:

lolE

0.973

lolC

0.951

lolA

0.889

macB

0.836

rpsK

0.795

oppD_1

0.743

DR95_2610

0.731

pheS

0.639

rpsE

0.635

serB

0.619

Your Current Organism:

Proteus vulgaris

NCBI taxonomy Id: 585
Other names: ATCC 29905, CCUG 35382, CCUG 39507, CDC PR1, CIP 104989, DSM 13387, LMG 16708, LMG:16708, NCTC 13145, P. vulgaris, strain PR 1

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
DR95_2610	lolA	DR95_2610	DR95_1413	ftsX-like permease family protein.	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	0.734
DR95_2610	lolD	DR95_2610	DR95_1204	ftsX-like permease family protein.	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	0.731
DR95_2610	macB	DR95_2610	DR95_1424	ftsX-like permease family protein.	Macrolide export ATP-binding/permease protein MacB; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.	0.913
lolA	DR95_2610	DR95_1413	DR95_2610	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	ftsX-like permease family protein.	0.734
lolA	lolC	DR95_1413	DR95_1205	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	Lipo-releasing system transmembrane protein lolC.	0.806
lolA	lolD	DR95_1413	DR95_1204	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	0.889
lolA	lolE	DR95_1413	DR95_1203	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	lolE_release: liporeleasing system, transmembrane protein LolE.	0.829
lolA	macB	DR95_1413	DR95_1424	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	Macrolide export ATP-binding/permease protein MacB; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.	0.847
lolC	lolA	DR95_1205	DR95_1413	Lipo-releasing system transmembrane protein lolC.	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	0.806
lolC	lolD	DR95_1205	DR95_1204	Lipo-releasing system transmembrane protein lolC.	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	0.951
lolC	lolE	DR95_1205	DR95_1203	Lipo-releasing system transmembrane protein lolC.	lolE_release: liporeleasing system, transmembrane protein LolE.	0.715
lolC	macB	DR95_1205	DR95_1424	Lipo-releasing system transmembrane protein lolC.	Macrolide export ATP-binding/permease protein MacB; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.	0.913
lolD	DR95_2610	DR95_1204	DR95_2610	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	ftsX-like permease family protein.	0.731
lolD	lolA	DR95_1204	DR95_1413	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	Outer membrane lipocarrier protein LolA; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).	0.889
lolD	lolC	DR95_1204	DR95_1205	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	Lipo-releasing system transmembrane protein lolC.	0.951
lolD	lolE	DR95_1204	DR95_1203	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	lolE_release: liporeleasing system, transmembrane protein LolE.	0.973
lolD	macB	DR95_1204	DR95_1424	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	Macrolide export ATP-binding/permease protein MacB; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.	0.836
lolD	oppD_1	DR95_1204	DR95_997	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	Hypothetical protein; oligo_HPY: oligopeptide/dipeptide ABC transporter, ATP-binding, C-terminal domain protein; Belongs to the ABC transporter superfamily.	0.743
lolD	pheS	DR95_1204	DR95_1068	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	pheS: phenylalanine--tRNA ligase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.	0.639
lolD	rpsE	DR95_1204	DR95_2126	Liporeleasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner.	Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family.	0.635

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