UniProt functional annotation for I6Y9J2



	UniProt functional annotation for I6Y9J2

UniProt code: I6Y9J2.

Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.

Function: 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. {ECO:0000269|PubMed:24041897}.

Activity regulation: Is irreversibly inactivated by the beta-lactams carbapenems via the formation of a covalent adduct resulting from acylation of the catalytic Cys; imipenem is the most efficient drug for in vitro LdtMt2 inactivation. {ECO:0000269|PubMed:23519417, ECO:0000269|PubMed:24041897}.

Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.

Subcellular location: Cell membrane {ECO:0000255|PROSITE- ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.

Domain: Consists of two tandem immunoglobulin-like Big_5 domains in the N-terminal region (residues 56-145 and 150-250), followed by a L,D- transpeptidase catalytic domain (residues 251-378) and a C-terminal tail (residues 379-408). {ECO:0000269|PubMed:23519417, ECO:0000269|PubMed:23519418}.

Miscellaneous: The peptidoglycan structure of stationary-phase M.tuberculosis is atypical since it contains a majority (80%) of 3->3 cross-links synthesized by L,D-transpeptidases that predominate over the 4->3 cross-links formed by the D,D-transpeptidase activity of classical penicillin-binding proteins (PubMed:18408028). In fact, 3-3 cross-linkages predominate throughout all growth phases and the ratio of 4-3/3-3 linkages does not vary significantly under any growth condition (PubMed:22906310).

Annotations taken from UniProtKB at the EBI.


Organism:		Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.



Function:		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. {ECO:0000269\|PubMed:24041897}.


Activity regulation:		Is irreversibly inactivated by the beta-lactams carbapenems via the formation of a covalent adduct resulting from acylation of the catalytic Cys; imipenem is the most efficient drug for in vitro LdtMt2 inactivation. {ECO:0000269\|PubMed:23519417, ECO:0000269\|PubMed:24041897}.
Pathway:		Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular location:		Cell membrane {ECO:0000255\|PROSITE- ProRule:PRU00303}; Lipid-anchor {ECO:0000255\|PROSITE-ProRule:PRU00303}.
Domain:		Consists of two tandem immunoglobulin-like Big_5 domains in the N-terminal region (residues 56-145 and 150-250), followed by a L,D- transpeptidase catalytic domain (residues 251-378) and a C-terminal tail (residues 379-408). {ECO:0000269\|PubMed:23519417, ECO:0000269\|PubMed:23519418}.
Miscellaneous:		The peptidoglycan structure of stationary-phase M.tuberculosis is atypical since it contains a majority (80%) of 3->3 cross-links synthesized by L,D-transpeptidases that predominate over the 4->3 cross-links formed by the D,D-transpeptidase activity of classical penicillin-binding proteins (PubMed:18408028). In fact, 3-3 cross-linkages predominate throughout all growth phases and the ratio of 4-3/3-3 linkages does not vary significantly under any growth condition (PubMed:22906310).