Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373379   51 RPHQGVDILCSAGSTVYAPFTGMIVGQEkpyqNKNAINNGVRIS-GRGFCVKMFYIKPI--KYKGPIKKGEKLGTLLPLQ 127
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAG----WLGGYGNLVIIDhGNGYSTLYAHLSSIlvKVGQRVKAGQVIGTVGSTG 76

                          90       100
                  ....*....|....*....|...
gi 317373379  128 KVYpgiQSHVHIE---NCDSSDP 147
Cdd:pfam01551  77 RST---GPHLHFEirkNGKPVDP 96

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373379   51 RPHQGVDILCSAGSTVYAPFTGMIVGQEkpyqNKNAINNGVRIS-GRGFCVKMFYIKPI--KYKGPIKKGEKLGTLLPLQ 127
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAG----WLGGYGNLVIIDhGNGYSTLYAHLSSIlvKVGQRVKAGQVIGTVGSTG 76

                          90       100
                  ....*....|....*....|...
gi 317373379  128 KVYpgiQSHVHIE---NCDSSDP 147
Cdd:pfam01551  77 RST---GPHLHFEirkNGKPVDP 96

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373379  53 HQGVDILCSAGSTVYAPFTGMIV--GQEKPYqnknaiNNGVRI-SGRGFCVKMFYIKPIKYK-G-PIKKGEKLGT 122
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVfaGWDGGY------GNYVIIdHGNGYYTLYAHLSSILVKvGqRVKKGQVIGT 69

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373379   51 RPHQGVDILCSAGSTVYAPFTGMIVGQEkpyqNKNAINNGVRIS-GRGFCVKMFYIKPI--KYKGPIKKGEKLGTLLPLQ 127
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAG----WLGGYGNLVIIDhGNGYSTLYAHLSSIlvKVGQRVKAGQVIGTVGSTG 76

                          90       100
                  ....*....|....*....|...
gi 317373379  128 KVYpgiQSHVHIE---NCDSSDP 147
Cdd:pfam01551  77 RST---GPHLHFEirkNGKPVDP 96

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373379  53 HQGVDILCSAGSTVYAPFTGMIV--GQEKPYqnknaiNNGVRI-SGRGFCVKMFYIKPIKYK-G-PIKKGEKLGT 122
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVfaGWDGGY------GNYVIIdHGNGYYTLYAHLSSILVKvGqRVKKGQVIGT 69