mltF protein (Alcanivorax borkumensis) - STRING interaction network

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mltF

Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...] (467 aa)

Predicted Functional Partners:

ABO_1221

0.564

ABO_1587

0.520

purL

0.482

ABO_0520

0.458

ABO_2284

0.454

Your Current Organism:

Alcanivorax borkumensis

NCBI taxonomy Id: 393595
Other names: A. borkumensis SK2, Alcanivorax borkumensis SK2, Alcanivorax borkumensis str. SK2, Alcanivorax borkumensis strain SK2

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ABO_0520	ABO_1221	ABO_0520	ABO_1221	Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.	Membrane-bound lytic murein transglycosylase D; Identified by match to PFAM protein family HMMPF01464 InterPro: SLT domain; High confidence in function and specificity.	0.410
ABO_0520	ABO_2284	ABO_0520	ABO_2284	Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.	Conserved hypothetical protein; Identified by Glimmer2; putative.	0.416
ABO_0520	mltF	ABO_0520	ABO_0784	Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	0.458
ABO_1221	ABO_0520	ABO_1221	ABO_0520	Membrane-bound lytic murein transglycosylase D; Identified by match to PFAM protein family HMMPF01464 InterPro: SLT domain; High confidence in function and specificity.	Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.	0.410
ABO_1221	mltF	ABO_1221	ABO_0784	Membrane-bound lytic murein transglycosylase D; Identified by match to PFAM protein family HMMPF01464 InterPro: SLT domain; High confidence in function and specificity.	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	0.564
ABO_1587	mltF	ABO_1587	ABO_0784	Soluble lytic transglycosylase, putative; Identified by sequencesimilarity; putative InterPro: SLT domain murein-degrading enzyme; High confidence in function and specificity.	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	0.520
ABO_2284	ABO_0520	ABO_2284	ABO_0520	Conserved hypothetical protein; Identified by Glimmer2; putative.	Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.	0.416
ABO_2284	mltF	ABO_2284	ABO_0784	Conserved hypothetical protein; Identified by Glimmer2; putative.	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	0.454
mltF	ABO_0520	ABO_0784	ABO_0520	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.	0.458
mltF	ABO_1221	ABO_0784	ABO_1221	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	Membrane-bound lytic murein transglycosylase D; Identified by match to PFAM protein family HMMPF01464 InterPro: SLT domain; High confidence in function and specificity.	0.564
mltF	ABO_1587	ABO_0784	ABO_1587	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	Soluble lytic transglycosylase, putative; Identified by sequencesimilarity; putative InterPro: SLT domain murein-degrading enzyme; High confidence in function and specificity.	0.520
mltF	ABO_2284	ABO_0784	ABO_2284	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	Conserved hypothetical protein; Identified by Glimmer2; putative.	0.454
mltF	purL	ABO_0784	ABO_0785	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.	0.482
purL	mltF	ABO_0785	ABO_0784	Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.	Periplasmic binding domain/transglycosylase SLTdomain fusion; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding prot [...]	0.482

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