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.

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 [...]

Membrane-bound lytic murein transglycosylase D; Identified by match to PFAM protein family HMMPF01464 InterPro: SLT domain; High confidence in function and specificity.

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; High confidence in function and specificity.

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 [...]

Soluble lytic transglycosylase, putative; Identified by sequencesimilarity; putative InterPro: SLT domain murein-degrading enzyme; High confidence in function and specificity.

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; High confidence in function and specificity.

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 [...]

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.

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 [...]

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; High confidence in function and specificity.

Membrane-bound lytic murein transglycosylase D; Identified by match to PFAM protein family HMMPF01464 InterPro: SLT domain; High confidence in function and specificity.

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; High confidence in function and specificity.

Soluble lytic transglycosylase, putative; Identified by sequencesimilarity; putative InterPro: SLT domain murein-degrading enzyme; High confidence in function and specificity.

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; 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 [...]

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; High confidence in function and specificity.

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 [...]

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 [...]

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 [...]

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 [...]

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 [...]

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; 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 [...]

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.

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.

N-acetylmuramoyl-L-alanine amidase; Identified by sequencesimilarity; putative InterPro: Cell wall hydrolase/autolysin; High confidence in function and specificity.

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 [...]