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Conserved domains on  [gi|446189521|ref|WP_000267376|]
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MULTISPECIES: M23 family metallopeptidase [Leptospira]

Protein Classification

LysM peptidoglycan-binding domain-containing M23 family metallopeptidase( domain architecture ID 12021290)

LysM peptidoglycan-binding domain-containing protein/M23 family metallopeptidase may bind N-acetylglucosamine in carbohydrates such as chitin, chitio-oligosaccharides and peptidoglycan, and/or lyse bacterial cell wall peptidoglycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 196-312 1.08e-61

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 195.19  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 196 LNARVTSRYGRRKDPFhTGSGGFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQ 275
Cdd:COG0739   75 VKGRITSGFGYRRHPV-TGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKV 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446189521 276 GTRVNTGTVIGAIGRTGSATGPHLHFEVFLNGNRVNP 312
Cdd:COG0739  154 GQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDP 190
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 131-174 5.56e-10

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


:

Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 53.94  E-value: 5.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446189521  131 YVVKPKDSLSKIAREMKTSVQKIVSANGLkKNSTLQVGLNLSIP 174
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKIP 43
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 196-312 1.08e-61

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 195.19  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 196 LNARVTSRYGRRKDPFhTGSGGFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQ 275
Cdd:COG0739   75 VKGRITSGFGYRRHPV-TGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKV 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446189521 276 GTRVNTGTVIGAIGRTGSATGPHLHFEVFLNGNRVNP 312
Cdd:COG0739  154 GQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDP 190
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 217-312 2.27e-47

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.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 155.01  E-value: 2.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521  217 GFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGTRVNTGTVIGAIGRTGSATG 296
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 446189521  297 PHLHFEVFLNGNRVNP 312
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 219-303 4.98e-41

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.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 138.11  E-value: 4.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 219 HTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGTRVNTGTVIGAIGRTGSATGPH 298
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                 ....*
gi 446189521 299 LHFEV 303
Cdd:cd12797   81 LHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 199-312 6.46e-24

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 101.28  E-value: 6.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 199 RVTSRYG-RRKDPFhTGSGGFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGT 277
Cdd:PRK11649 293 RISSNFNpRRLNPV-TGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQ 371

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446189521 278 RVNTGTVIGAIGRTGSATGPHLHFEVFLNGNRVNP 312
Cdd:PRK11649 372 KVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNP 406
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 131-174 5.56e-10

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 53.94  E-value: 5.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446189521  131 YVVKPKDSLSKIAREMKTSVQKIVSANGLkKNSTLQVGLNLSIP 174
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
116-175 1.51e-09

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 56.26  E-value: 1.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 116 ISSKIVNHSGIIYKNYVVKPKDSLSKIAREMKTSVQKIVSANGLkKNSTLQVGLNLSIPV 175
Cdd:COG1388   97 IARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKIPA 155
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 131-173 1.58e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 52.87  E-value: 1.58e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446189521 131 YVVKPKDSLSKIAREMKTSVQKIVSANGLKKNSTLQVGLNLSI 173
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
131-173 2.50e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.06  E-value: 2.50e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 446189521   131 YVVKPKDSLSKIAREMKTSVQKIVSANGLKKNSTLQVGLNLSI 173
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 115-173 3.30e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 42.03  E-value: 3.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446189521 115 VISSKIVNHSGIIYKNYVVKPKDSLSKIAREMKTSVQKIVSANGLkKNSTLQVGLNLSI 173
Cdd:PRK10783 330 VQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNL-RGSKLKVGQTLTI 387
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 196-312 1.08e-61

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 195.19  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 196 LNARVTSRYGRRKDPFhTGSGGFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQ 275
Cdd:COG0739   75 VKGRITSGFGYRRHPV-TGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKV 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446189521 276 GTRVNTGTVIGAIGRTGSATGPHLHFEVFLNGNRVNP 312
Cdd:COG0739  154 GQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDP 190
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 217-312 2.27e-47

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.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 155.01  E-value: 2.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521  217 GFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGTRVNTGTVIGAIGRTGSATG 296
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 446189521  297 PHLHFEVFLNGNRVNP 312
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 194-312 6.48e-43

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 152.23  E-value: 6.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 194 PVlNARVTSRYGRRKdpfhtGSGGFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITI 273
Cdd:COG4942  258 PV-SGRVVRRFGERD-----GGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLV 331

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446189521 274 EQGTRVNTGTVIGAIGRTGSATGPHLHFEVFLNGNRVNP 312
Cdd:COG4942  332 KVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDP 370
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 219-303 4.98e-41

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.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 138.11  E-value: 4.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 219 HTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGTRVNTGTVIGAIGRTGSATGPH 298
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                 ....*
gi 446189521 299 LHFEV 303
Cdd:cd12797   81 LHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 191-312 7.76e-36

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 128.61  E-value: 7.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 191 FVHPVlNARVTSRYGRR--KDPFhTGSGGFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAH- 267
Cdd:COG5821   69 FLKPV-SGKITREFGEDlvYSKT-LNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANl 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446189521 268 CSKITIEQGTRVNTGTVIGAIGRTG---SATGPHLHFEVFLNGNRVNP 312
Cdd:COG5821  147 DSKIKVKVGQKVKKGQVIGKVGSTAlfeSSEGPHLHFEVLKNGKPVDP 194
PRK11649 PRK11649
putative peptidase; Provisional
 199-312 6.46e-24

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 101.28  E-value: 6.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 199 RVTSRYG-RRKDPFhTGSGGFHTGLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGT 277
Cdd:PRK11649 293 RISSNFNpRRLNPV-TGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQ 371

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446189521 278 RVNTGTVIGAIGRTGSATGPHLHFEVFLNGNRVNP 312
Cdd:PRK11649 372 KVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNP 406
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 219-318 8.79e-20

Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444522 [Multi-domain]  Cd Length: 224  Bit Score: 86.13  E-value: 8.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 219 HTGLDFAGAQGAP--ILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGTRVNTGTVIGAIGRT--GSA 294
Cdd:COG5820  120 STGIDIAAKDGESfdVLAALSGTVTEVEEDPLLGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGTAGRNlfNKD 199

                         90       100
                 ....*....|....*....|....
gi 446189521 295 TGPHLHFEVFLNGNRVNPDVALKK 318
Cdd:COG5820  200 AGVHLHFEVRKDGKAVNPESYLPK 223
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 173-312 1.15e-18

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 83.12  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 173 IPVQVRNASREKVEfhKLFVHPVlNARVTSRYGrrkdpfHTGSGgfhtgLDFAGAQGAPILASADGVVSFAGVNGGYGNT 252
Cdd:COG5833   88 LPPFGKEEETVEQG--EAFALPV-SGKVVESFQ------ENGKG-----VDIETPGGANVKAVKEGYVIFAGKDEETGKT 153

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 253 VIIDHDNGYKTMYAHCSKITIEQGTRVNTGTVIGAIGRTGSATGpHLHFEVFLNGNRVNP 312
Cdd:COG5833  154 VIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPATEGEEG-TFYFAIKKGGKFIDP 212
nlpD PRK10871
murein hydrolase activator NlpD;
205-312 9.05e-17

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 79.49  E-value: 9.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 205 GRRKDPFHTGSGGfHTGLDFAGAQGAPILASADGVVSFAGvNG--GYGNTVIIDHDNGYKTMYAHCSKITIEQGTRVNTG 282
Cdd:PRK10871 206 GKVIENFSASEGG-NKGIDIAGSKGQAIIATADGRVVYAG-NAlrGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAG 283

                         90       100       110
                 ....*....|....*....|....*....|
gi 446189521 283 TVIGAIGRTGSATgPHLHFEVFLNGNRVNP 312
Cdd:PRK10871 284 QKIATMGSTGTSS-TRLHFEIRYKGKSVNP 312
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 131-174 5.56e-10

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 53.94  E-value: 5.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446189521  131 YVVKPKDSLSKIAREMKTSVQKIVSANGLkKNSTLQVGLNLSIP 174
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
116-175 1.51e-09

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 56.26  E-value: 1.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 116 ISSKIVNHSGIIYKNYVVKPKDSLSKIAREMKTSVQKIVSANGLkKNSTLQVGLNLSIPV 175
Cdd:COG1388   97 IARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKIPA 155
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 131-173 1.58e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 52.87  E-value: 1.58e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446189521 131 YVVKPKDSLSKIAREMKTSVQKIVSANGLKKNSTLQVGLNLSI 173
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
131-173 2.50e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.06  E-value: 2.50e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 446189521   131 YVVKPKDSLSKIAREMKTSVQKIVSANGLKKNSTLQVGLNLSI 173
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
PRK11637 PRK11637
AmiB activator; Provisional
 221-312 4.43e-07

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 51.23  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521 221 GLDFAGAQGAPILASADGVVSFAGVNGGYGNTVIIDHDNGYKTMYAHCSKITIEQGTRVNTGTVIGAIGRTGSATGPHLH 300
Cdd:PRK11637 331 GMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLY 410

                         90
                 ....*....|..
gi 446189521 301 FEVFLNGNRVNP 312
Cdd:PRK11637 411 FEIRRQGQAVNP 422
PRK06148 PRK06148
hypothetical protein; Provisional
 219-303 1.46e-05

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 46.94  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446189521  219 HTGLDFAGAQGAPILASADGVVSFAGVNG---GYGNTVIIDH--DNG--YKTMYAHCSKITIEQ---GTRVNTGTVIGAI 288
Cdd:PRK06148  441 HLGVDLFAPAGTPVYAPLAGTVRSVEIEAvplGYGGLVALEHetPGGdpFYTLYGHLAHEAVSRlkpGDRLAAGELFGAM 520

                          90
                  ....*....|....*..
gi 446189521  289 GRTGSATG--PHLHFEV 303
Cdd:PRK06148  521 GDAHENGGwaPHLHFQL 537
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 115-173 3.30e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 42.03  E-value: 3.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446189521 115 VISSKIVNHSGIIYKNYVVKPKDSLSKIAREMKTSVQKIVSANGLkKNSTLQVGLNLSI 173
Cdd:PRK10783 330 VQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNL-RGSKLKVGQTLTI 387
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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