Conserved hypothetical protein; Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems.

Penicillin-insensitive transglycosylase; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits) (By similarity). Has little peptidoglycan hydrolytic activity; however it inhibits the synergistic peptidoglycan hydrolysis of RipA plus RpfB.

Possible conserved exported protein; Probable L,D-transpeptidase that may perform as-yet-unknown cross-linking reactions in M.tuberculosis. Is not able to generate 3->3 cross-links in peptidoglycan, using tetrapeptide stems as acyl donor substrates. May function in the anchoring of proteins to peptidoglycan.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Possible conserved exported protein; Probable L,D-transpeptidase that may perform as-yet-unknown cross-linking reactions in M.tuberculosis. Is not able to generate 3->3 cross-links in peptidoglycan, using tetrapeptide stems as acyl donor substrates. May function in the anchoring of proteins to peptidoglycan.

Conserved protein; Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. Belongs to the peptidase S13 family.

Possible conserved exported protein; Probable L,D-transpeptidase that may perform as-yet-unknown cross-linking reactions in M.tuberculosis. Is not able to generate 3->3 cross-links in peptidoglycan, using tetrapeptide stems as acyl donor substrates. May function in the anchoring of proteins to peptidoglycan.

Probable peptidoglycan hydrolase; Cell-wall hydrolase that hydrolyzes the amide bond between N- acetylmuramic acid and L-alanine in cell-wall glycopeptides. Is able to lyse whole mycobacteria, release peptidoglycan from the cell wall of M.luteus and M.smegmatis, and cleave N-acetylmuramoyl-L-alanyl-D- isoglutamine, releasing free N-acetylmuramic acid and dipeptide.

Possible conserved exported protein; Probable L,D-transpeptidase that may perform as-yet-unknown cross-linking reactions in M.tuberculosis. Is not able to generate 3->3 cross-links in peptidoglycan, using tetrapeptide stems as acyl donor substrates. May function in the anchoring of proteins to peptidoglycan.

Probable conserved lipoprotein LprQ; Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems.

Possible conserved exported protein; Probable L,D-transpeptidase that may perform as-yet-unknown cross-linking reactions in M.tuberculosis. Is not able to generate 3->3 cross-links in peptidoglycan, using tetrapeptide stems as acyl donor substrates. May function in the anchoring of proteins to peptidoglycan.

Peptidoglycan hydrolase; Peptidoglycan endopeptidase that cleaves the bond between D- glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages. Belongs to the peptidase C40 family.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Possible conserved exported protein; Probable L,D-transpeptidase that may perform as-yet-unknown cross-linking reactions in M.tuberculosis. Is not able to generate 3->3 cross-links in peptidoglycan, using tetrapeptide stems as acyl donor substrates. May function in the anchoring of proteins to peptidoglycan.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Possible arabinofuranosyltransferase AftB; Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. Catalyzes the transfer of arabinofuranosyl (Araf) residues from the sugar donor decaprenyl-phospho-arabinose (DPA) to the arabinan domain to form terminal beta-(1->2)-linked Araf residues, which marks the end point for AG arabinan biosynthesis before decoration with mycolic acids.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Possible arabinofuranosyltransferase AftC; Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. Catalyzes the addition of an arabinofuranosyl (Araf) residue from the sugar donor decaprenyl-phospho-arabinose (DPA) on the C-3 of an alpha-(1->5)-linked Araf from the arabinan backbone of AG. It can also use (Z,Z)- farnesylphosphoryl D-arabinose (Z-FPA), and to a lesser extent (E,E,Z,Z,Z,Z)-heptaprenylphosphoryl D-arabinose (Z-HPA) and (Z)- nerylphosphoryl D-arabinos [...]

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Probable arabinosyltransferase A; Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Probable arabinosyltransferase B; Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan; Belongs to the emb family.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Probable arabinosyltransferase C; Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Probable conserved lipoprotein LpqI; Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptidoglycan fragments. Acts as a regulator for GlcNAc-MurNAc levels by cleaving disaccharides and allowing the breakdown of MurNAc.

Conserved hypothetical protein. Secreted; May function as a peptidoglycan hydrolase with glycosidase activity. In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4).

Peptidoglycan hydrolase; Peptidoglycan endopeptidase that cleaves the bond between D- glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages. Belongs to the peptidase C40 family.

Conserved protein; Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. Belongs to the peptidase S13 family.

Possible conserved exported protein; Probable L,D-transpeptidase that may perform as-yet-unknown cross-linking reactions in M.tuberculosis. Is not able to generate 3->3 cross-links in peptidoglycan, using tetrapeptide stems as acyl donor substrates. May function in the anchoring of proteins to peptidoglycan.

Conserved protein; Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. Belongs to the peptidase S13 family.

Conserved hypothetical protein; Cell-wall hydrolase that hydrolyzes the amide bond between N- acetylmuramic acid and L-alanine in cell-wall glycopeptides. Is able to hydrolyze the cell walls of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli DH5alpha, E.aerogenes, L.acidophilus, B.thuringiensis, B.pumilus, B.subtilis and E.coli W3110), thereby showing that it is a cell-wall hydrolase with broad-spectrum activity. May have a role in peptidoglycan fragment recycling. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Conserved protein; Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. Belongs to the peptidase S13 family.

Probable peptidoglycan hydrolase; Cell-wall hydrolase that hydrolyzes the amide bond between N- acetylmuramic acid and L-alanine in cell-wall glycopeptides. Is able to lyse whole mycobacteria, release peptidoglycan from the cell wall of M.luteus and M.smegmatis, and cleave N-acetylmuramoyl-L-alanyl-D- isoglutamine, releasing free N-acetylmuramic acid and dipeptide.

Conserved protein; Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. Belongs to the peptidase S13 family.

Probable penicillin-binding protein PbpA; Cell wall formation. Plays an important role in cell division and cell shape maintenance by cross-linking adjacent peptidoglycan chains through transpeptidation; Belongs to the transpeptidase family.

Conserved protein; Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. Belongs to the peptidase S13 family.

Probable penicillin-binding membrane protein PbpB; Synthesis of cross-linked peptidoglycan from the lipid intermediates; Belongs to the transpeptidase family.

Conserved protein; Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. Belongs to the peptidase S13 family.

Penicillin-insensitive transglycosylase; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits) (By similarity). Has little peptidoglycan hydrolytic activity; however it inhibits the synergistic peptidoglycan hydrolysis of RipA plus RpfB.