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Conserved domains on  [gi|2225545426|ref|WP_245557936|]
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M23 family metallopeptidase [Deinococcus apachensis]

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 ...
 113-307 1.09e-51

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: 169.00  E-value: 1.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 113 SQLLRANPQIDAGRPLRAGVTVRIPGRNVAARLPSTASRTPAARSASRPAQGATVRSASIRVSAVPSASGWLWPVAGYry 192
Cdd:COG0739     1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 193 ISSGFGERN--IDGDHEMHYGVDIVAPEGTNVRAARSGRVleSRADFERGWGWTVVIEHPDGWITRYAHLSANLARAGDR 270
Cdd:COG0739    79 ITSGFGYRRhpVTGRRRFHKGIDIAAPTGTPVYAAADGTV--VFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQR 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2225545426 271 VVRGQLIGRVGNTGRSTGPHLHFGTYLRWNPKDPLRL 307
Cdd:COG0739   157 VKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPF 193
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 40-84 2.94e-11

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: 57.41  E-value: 2.94e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2225545426  40 YRVRSGDNLTTIARRAGISISALKAANpKLRNaDHVEAGQVLRIP 84
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSS-PNLYVGQKLKIP 43
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 93-129 3.70e-04

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: 37.38  E-value: 3.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2225545426  93 HRVKSGENLTVIAHRYSFTLSQLLRAN----PQIDAGRPLR 129
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNglssPNLYVGQKLK 41
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 113-307 1.09e-51

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: 169.00  E-value: 1.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 113 SQLLRANPQIDAGRPLRAGVTVRIPGRNVAARLPSTASRTPAARSASRPAQGATVRSASIRVSAVPSASGWLWPVAGYry 192
Cdd:COG0739     1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 193 ISSGFGERN--IDGDHEMHYGVDIVAPEGTNVRAARSGRVleSRADFERGWGWTVVIEHPDGWITRYAHLSANLARAGDR 270
Cdd:COG0739    79 ITSGFGYRRhpVTGRRRFHKGIDIAAPTGTPVYAAADGTV--VFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQR 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2225545426 271 VVRGQLIGRVGNTGRSTGPHLHFGTYLRWNPKDPLRL 307
Cdd:COG0739   157 VKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPF 193
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 207-304 9.70e-41

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: 137.29  E-value: 9.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 207 EMHYGVDIVAPEGTNVRAARSGRVLEsrADFERGWGWTVVIEHPDGWITRYAHLSANLARAGDRVVRGQLIGRVGNTGRS 286
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVF--AGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRS 78

                          90
                  ....*....|....*...
gi 2225545426 287 TGPHLHFGTYLRWNPKDP 304
Cdd:pfam01551  79 TGPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 209-294 4.15e-39

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: 132.72  E-value: 4.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 209 HYGVDIVAPEGTNVRAARSGRVLESRADfeRGWGWTVVIEHPDGWITRYAHLSANLARAGDRVVRGQLIGRVGNTGRSTG 288
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD--GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTG 78


                  ....*.
gi 2225545426 289 PHLHFG 294
Cdd:cd12797    79 PHLHFE 84
PRK11649 PRK11649
putative peptidase; Provisional
 180-305 1.10e-18

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 85.87  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 180 ASGWL-WPVAGYRYISSGFGERNID---GDHEMHYGVDIVAPEGTNVRAARSGRVLESRadFERGWGWTVVIEHPDGWIT 255
Cdd:PRK11649  280 AKGFLrFPTAKQFRISSNFNPRRLNpvtGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAK--RSGAAGNYVAIRHGRQYTT 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2225545426 256 RYAHLSANLARAGDRVVRGQLIGRVGNTGRSTGPHLHFGTYLRWNPKDPL 305
Cdd:PRK11649  358 RYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPL 407
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 40-84 2.94e-11

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: 57.41  E-value: 2.94e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2225545426  40 YRVRSGDNLTTIARRAGISISALKAANpKLRNaDHVEAGQVLRIP 84
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSS-PNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 40-83 3.52e-11

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: 57.11  E-value: 3.52e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2225545426  40 YRVRSGDNLTTIARRAGISISALKAANPkLRNADHVEAGQVLRI 83
Cdd:cd00118     3 YTVKPGDTLWSIAKKYGVTVEELAAANP-LINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
40-83 1.54e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 55.53  E-value: 1.54e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2225545426   40 YRVRSGDNLTTIARRAGISISALKAANPKLrNADHVEAGQVLRI 83
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNIL-DPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
34-86 3.45e-10

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 57.80  E-value: 3.45e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2225545426  34 ASAATNYRVRSGDNLTTIARRAGISISALKAANpKLRNaDHVEAGQVLRIPNR 86
Cdd:COG1388   106 APSPVTYTVKKGDTLWSIARRYGVSVEELKRWN-GLSS-DTIRPGQKLKIPAS 156
LysM smart00257
Lysin motif;
92-136 1.25e-04

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 38.97  E-value: 1.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2225545426   92 THRVKSGENLTVIAHRYSFTLSQLLRANPQIDAGRpLRAGVTVRI 136
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDN-LQVGQKLKI 44
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 28-84 3.17e-04

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 40.28  E-value: 3.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225545426  28 LVLAGLASAATNYRVRSGDNLTTIARRA---GISISALKAAN-PKLRNADHVEAGQVLRIP 84
Cdd:PRK11198   86 VKVATPAPESQFYTVKSGDTLSAIAKKVygnANKYNKIFEANkPMLKSPDKIYPGQVLRIP 146
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 93-129 3.70e-04

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: 37.38  E-value: 3.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2225545426  93 HRVKSGENLTVIAHRYSFTLSQLLRAN----PQIDAGRPLR 129
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNglssPNLYVGQKLK 41
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 113-307 1.09e-51

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: 169.00  E-value: 1.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 113 SQLLRANPQIDAGRPLRAGVTVRIPGRNVAARLPSTASRTPAARSASRPAQGATVRSASIRVSAVPSASGWLWPVAGYry 192
Cdd:COG0739     1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 193 ISSGFGERN--IDGDHEMHYGVDIVAPEGTNVRAARSGRVleSRADFERGWGWTVVIEHPDGWITRYAHLSANLARAGDR 270
Cdd:COG0739    79 ITSGFGYRRhpVTGRRRFHKGIDIAAPTGTPVYAAADGTV--VFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQR 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2225545426 271 VVRGQLIGRVGNTGRSTGPHLHFGTYLRWNPKDPLRL 307
Cdd:COG0739   157 VKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPF 193
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 207-304 9.70e-41

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: 137.29  E-value: 9.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 207 EMHYGVDIVAPEGTNVRAARSGRVLEsrADFERGWGWTVVIEHPDGWITRYAHLSANLARAGDRVVRGQLIGRVGNTGRS 286
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVF--AGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRS 78

                          90
                  ....*....|....*...
gi 2225545426 287 TGPHLHFGTYLRWNPKDP 304
Cdd:pfam01551  79 TGPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 209-294 4.15e-39

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: 132.72  E-value: 4.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 209 HYGVDIVAPEGTNVRAARSGRVLESRADfeRGWGWTVVIEHPDGWITRYAHLSANLARAGDRVVRGQLIGRVGNTGRSTG 288
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD--GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTG 78


                  ....*.
gi 2225545426 289 PHLHFG 294
Cdd:cd12797    79 PHLHFE 84
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-306 3.85e-35

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: 130.65  E-value: 3.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 162 AQGATVRSASIRVSAVPSASGWLWPVAGYryISSGFGERniDGDHEMHYGVDIVAPEGTNVRAARSGRVleSRADFERGW 241
Cdd:COG4942   234 AEAAAAAERTPAAGFAALKGKLPWPVSGR--VVRRFGER--DGGGGRNKGIDIAAPPGAPVRAVADGTV--VYAGWLRGY 307

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225545426 242 GWTVVIEHPDGWITRYAHLSANLARAGDRVVRGQLIGRVGNTGRSTGPHLHFGtyLRWN--PKDPLR 306
Cdd:COG4942   308 GNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFE--LRKNgkPVDPLP 372
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 174-305 1.78e-34

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: 124.37  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 174 VSAVPSASGWLWPVAGYryISSGFGERNID----GDHEMHYGVDIVAPEGTNVRAARSGRVLESRADFErgWGWTVVIEH 249
Cdd:COG5821    60 KVTASTSNKFLKPVSGK--ITREFGEDLVYsktlNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPK--YGITVVIDH 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 250 PDGWITRYAHLSAN-LARAGDRVVRGQLIGRVGNTGR---STGPHLHFGTYLRWNPKDPL 305
Cdd:COG5821   136 GNGIKTVYANLDSKiKVKVGQKVKKGQVIGKVGSTALfesSEGPHLHFEVLKNGKPVDPM 195
PRK11649 PRK11649
putative peptidase; Provisional
 180-305 1.10e-18

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 85.87  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 180 ASGWL-WPVAGYRYISSGFGERNID---GDHEMHYGVDIVAPEGTNVRAARSGRVLESRadFERGWGWTVVIEHPDGWIT 255
Cdd:PRK11649  280 AKGFLrFPTAKQFRISSNFNPRRLNpvtGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAK--RSGAAGNYVAIRHGRQYTT 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2225545426 256 RYAHLSANLARAGDRVVRGQLIGRVGNTGRSTGPHLHFGTYLRWNPKDPL 305
Cdd:PRK11649  358 RYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPL 407
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 175-294 2.46e-14

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 70.79  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 175 SAVPSASGWLWPVAGYryISSGFGErnidgDHEmhyGVDIVAPEGTNVRAARSGRVLEsrADFERGWGWTVVIEHPDGWI 254
Cdd:COG5833    96 ETVEQGEAFALPVSGK--VVESFQE-----NGK---GVDIETPGGANVKAVKEGYVIF--AGKDEETGKTVIIQHADGSE 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2225545426 255 TRYAHLSANLARAGDRVVRGQLIGRVGNTGRSTGpHLHFG 294
Cdd:COG5833   164 SWYGNLSSIDVKLYDFVEAGQKIGTVPATEGEEG-TFYFA 202
PRK11637 PRK11637
AmiB activator; Provisional
 184-293 3.25e-14

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 72.42  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 184 LWPVAGYryISSGFGERnIDGdhEMHY-GVDIVAPEGTNVRAARSGRVLesRADFERGWGWTVVIEHPDGWITRYAHLSA 262
Cdd:PRK11637  308 FWPVRGP--TLHRFGEQ-LQG--ELRWkGMVIGASEGTEVKAIADGRVL--LADWLQGYGLVVVVEHGKGDMSLYGYNQS 380

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2225545426 263 NLARAGDRVVRGQLIGRVGNTGRSTGPHLHF 293
Cdd:PRK11637  381 ALVSVGAQVRAGQPIALVGSSGGQGRPSLYF 411
PRK06148 PRK06148
hypothetical protein; Provisional
 122-293 1.39e-13

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 71.21  E-value: 1.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426  122 IDAGRPLRAGVTVRIPGRNVAARLPSTASRTPAArSASRPAQGATVRSASIRVSAVPSASGwLWPVAGYRYISSGFGERN 201
Cdd:PRK06148   355 LDANRGAFAPLVGPDLATLPKASVPVGDAAHPDS-AGQRPAEAAAWWDEFCARTGAQLGIG-PYGEPRLVYTDEAFTSRF 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426  202 IDGDHE-MHYGVDIVAPEGTNVRAARSGRVLESRADFER-GWGWTVVIEH--PDG--WITRYAHLSANLA---RAGDRVV 272
Cdd:PRK06148   433 IEGERRtVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAVPlGYGGLVALEHetPGGdpFYTLYGHLAHEAVsrlKPGDRLA 512

                          170       180
                   ....*....|....*....|...
gi 2225545426  273 RGQLIGRVGNTGRSTG--PHLHF 293
Cdd:PRK06148   513 AGELFGAMGDAHENGGwaPHLHF 535
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 40-84 2.94e-11

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: 57.41  E-value: 2.94e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2225545426  40 YRVRSGDNLTTIARRAGISISALKAANpKLRNaDHVEAGQVLRIP 84
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSS-PNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 40-83 3.52e-11

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: 57.11  E-value: 3.52e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2225545426  40 YRVRSGDNLTTIARRAGISISALKAANPkLRNADHVEAGQVLRI 83
Cdd:cd00118     3 YTVKPGDTLWSIAKKYGVTVEELAAANP-LINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
40-83 1.54e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 55.53  E-value: 1.54e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2225545426   40 YRVRSGDNLTTIARRAGISISALKAANPKLrNADHVEAGQVLRI 83
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNIL-DPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
34-86 3.45e-10

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 57.80  E-value: 3.45e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2225545426  34 ASAATNYRVRSGDNLTTIARRAGISISALKAANpKLRNaDHVEAGQVLRIPNR 86
Cdd:COG1388   106 APSPVTYTVKKGDTLWSIARRYGVSVEELKRWN-GLSS-DTIRPGQKLKIPAS 156
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 16-123 3.81e-10

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 60.52  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426  16 VAPARHLLATG-------VLVLAGLASAATNYRVRSGDNLTTIARRAGISISALKAANpKLRnADHVEAGQVLRIPNRQL 88
Cdd:PRK10783  315 ADQLRESLASGeiaavqsTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWN-NLR-GSKLKVGQTLTIGAGSS 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2225545426  89 PGQ--------THRVKSGENLTVIAHRYSFTLSQLLRANPQID 123
Cdd:PRK10783  393 AQRlannsdsiTYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTA 435
nlpD PRK10871
murein hydrolase activator NlpD;
140-306 3.62e-09

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 56.77  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 140 NVAARLPSTasrTPAARSASRPAQGATVRSASIRVSAVPSASgwlwPVAGYRYISSGFGERNIDGDHEMHYGVDIVAPEG 219
Cdd:PRK10871  157 SANKMLPNN---KPAATTVTAPVTAPTASTTEPTASSTSTST----PISTWRWPTDGKVIENFSASEGGNKGIDIAGSKG 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426 220 TNVRAARSGRVLESrADFERGWGWTVVIEHPDGWITRYAHLSANLARAGDRVVRGQLIGRVGNTGRSTgPHLHFGTYLRW 299
Cdd:PRK10871  230 QAIIATADGRVVYA-GNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS-TRLHFEIRYKG 307


                  ....*..
gi 2225545426 300 NPKDPLR 306
Cdd:PRK10871  308 KSVNPLR 314
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 91-136 1.90e-08

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: 49.79  E-value: 1.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2225545426  91 QTHRVKSGENLTVIAHRYSFTLSQLLRANPQIDAGRpLRAGVTVRI 136
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDC-IYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
3-139 2.61e-07

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 49.71  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426   3 SPLIQSPSRSRTWVAPARHLLATGVLVLAGLASAATNYRVRSGDNLTTIARRAGISISAlkaanpklrnadhveagqvlr 82
Cdd:COG1388    49 AAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAP--------------------- 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2225545426  83 ipnrqlPGQTHRVKSGENLTVIAHRYSFTLSQLLRANPQidAGRPLRAGVTVRIPGR 139
Cdd:COG1388   108 ------SPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL--SSDTIRPGQKLKIPAS 156
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 34-87 1.21e-06

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 47.69  E-value: 1.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2225545426  34 ASAATNYRVRSGDNLTTIARRA---GISISALKAAN-PKLRNADHVEAGQVLRIPNRQ 87
Cdd:COG1652   106 PDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrDQIKNPDLIYPGQVLRIPALE 163
LysM smart00257
Lysin motif;
92-136 1.25e-04

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 38.97  E-value: 1.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2225545426   92 THRVKSGENLTVIAHRYSFTLSQLLRANPQIDAGRpLRAGVTVRI 136
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDN-LQVGQKLKI 44
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 28-84 3.17e-04

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 40.28  E-value: 3.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225545426  28 LVLAGLASAATNYRVRSGDNLTTIARRA---GISISALKAAN-PKLRNADHVEAGQVLRIP 84
Cdd:PRK11198   86 VKVATPAPESQFYTVKSGDTLSAIAKKVygnANKYNKIFEANkPMLKSPDKIYPGQVLRIP 146
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 93-129 3.70e-04

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: 37.38  E-value: 3.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2225545426  93 HRVKSGENLTVIAHRYSFTLSQLLRAN----PQIDAGRPLR 129
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNglssPNLYVGQKLK 41
FimV COG3170
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
82-181 1.29e-03

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];


Pssm-ID: 442403 [Multi-domain]  Cd Length: 508  Bit Score: 40.16  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225545426  82 RIPNRQLPGQTHRVKSGENLTVIAHRYSF---------TLSQLLRANPQIDAGRP---LRAGVTVRIPGRN-VAARLPST 148
Cdd:COG3170   139 AEAAPAASGEYYPVRPGDTLWSIAARPVRpssgvsldqMMVALYRANPDAFIDGNinrLKAGAVLRVPAAEeVAALSPAE 218

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2225545426 149 ASRTPAARSASRPAQGATVRSAsirVSAVPSAS 181
Cdd:COG3170   219 ARQEVQAQSADWAAYRARLAAA---VEPAPAAA 248
 
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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