NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|697053799|ref|WP_033146405|]
View 

MULTISPECIES: murein hydrolase activator NlpD [Enterobacter]

Protein Classification

murein hydrolase activator NlpD( domain architecture ID 11485035)

murein hydrolase activator NlpD is required for septal murein cleavage and daughter cell separation during cell division

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
1-374 0e+00

murein hydrolase activator NlpD;


:

Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 552.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799   1 MSAGSPKFTISRVAALSLVSLWLAGCTSSNNAPAPvssvggnsgsgntsggmlitpppkmgtstaqqnppiqpvqrpmtq 80
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPAP--------------------------------------------- 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  81 ptqIQPVEqpvqtqNGRIVYNRQYGNIPKGSYTGgSTYTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPYGLEVGQTLQV 160
Cdd:PRK10871  36 ---VSSVG------NGRIVYNRQYGNIPKGSYSG-STYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQV 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 161 GNATGTPLTPGNTVSAADVTAQNNSVKPAQKSTTVVASQPVITYSEDSGDQTANKMLPNNKGTATVVTAPVTAPVVSSTE 240
Cdd:PRK10871 106 GNASGTPITGGNAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAATTVTAPVTAPTASTTE 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 241 PTASSMTSSSPISAWRWPTDGKVIENFSSSEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 320
Cdd:PRK10871 186 PTASSTSTSTPISTWRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 265

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697053799 321 YAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLQYLPQR 374
Cdd:PRK10871 266 YAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
1-374 0e+00

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 552.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799   1 MSAGSPKFTISRVAALSLVSLWLAGCTSSNNAPAPvssvggnsgsgntsggmlitpppkmgtstaqqnppiqpvqrpmtq 80
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPAP--------------------------------------------- 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  81 ptqIQPVEqpvqtqNGRIVYNRQYGNIPKGSYTGgSTYTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPYGLEVGQTLQV 160
Cdd:PRK10871  36 ---VSSVG------NGRIVYNRQYGNIPKGSYSG-STYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQV 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 161 GNATGTPLTPGNTVSAADVTAQNNSVKPAQKSTTVVASQPVITYSEDSGDQTANKMLPNNKGTATVVTAPVTAPVVSSTE 240
Cdd:PRK10871 106 GNASGTPITGGNAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAATTVTAPVTAPTASTTE 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 241 PTASSMTSSSPISAWRWPTDGKVIENFSSSEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 320
Cdd:PRK10871 186 PTASSTSTSTPISTWRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 265

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697053799 321 YAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLQYLPQR 374
Cdd:PRK10871 266 YAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 255-374 1.24e-50

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: 173.80  E-value: 1.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 255 WRWPTDGKVIENFSSSEGG---NKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 331
Cdd:COG4942  255 LPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLSSLLVKV 333

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 697053799 332 QQEVKAGQKIATMGSTG-TSSTRLHFEIRYKGKSVNPLQYLPQR 374
Cdd:COG4942  334 GQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGKPVDPLPWLAKR 377
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 272-367 4.20e-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: 139.99  E-value: 4.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  272 GGNKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 351
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 697053799  352 -TRLHFEIRYKGKSVNP 367
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 274-358 3.19e-30

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: 110.76  E-value: 3.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 274 NKGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS-T 352
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                 ....*.
gi 697053799 353 RLHFEI 358
Cdd:cd12797   80 HLHFEI 85
LysM smart00257
Lysin motif;
117-160 2.32e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.45  E-value: 2.32e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 697053799   117 TYTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPYGLEVGQTLQV 160
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
1-374 0e+00

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 552.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799   1 MSAGSPKFTISRVAALSLVSLWLAGCTSSNNAPAPvssvggnsgsgntsggmlitpppkmgtstaqqnppiqpvqrpmtq 80
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPAP--------------------------------------------- 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  81 ptqIQPVEqpvqtqNGRIVYNRQYGNIPKGSYTGgSTYTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPYGLEVGQTLQV 160
Cdd:PRK10871  36 ---VSSVG------NGRIVYNRQYGNIPKGSYSG-STYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQV 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 161 GNATGTPLTPGNTVSAADVTAQNNSVKPAQKSTTVVASQPVITYSEDSGDQTANKMLPNNKGTATVVTAPVTAPVVSSTE 240
Cdd:PRK10871 106 GNASGTPITGGNAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAATTVTAPVTAPTASTTE 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 241 PTASSMTSSSPISAWRWPTDGKVIENFSSSEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 320
Cdd:PRK10871 186 PTASSTSTSTPISTWRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 265

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697053799 321 YAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLQYLPQR 374
Cdd:PRK10871 266 YAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 255-374 1.24e-50

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: 173.80  E-value: 1.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 255 WRWPTDGKVIENFSSSEGG---NKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVRE 331
Cdd:COG4942  255 LPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLSSLLVKV 333

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 697053799 332 QQEVKAGQKIATMGSTG-TSSTRLHFEIRYKGKSVNPLQYLPQR 374
Cdd:COG4942  334 GQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGKPVDPLPWLAKR 377
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 228-373 6.85e-47

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: 158.60  E-value: 6.85e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 228 TAPVTAPVVSSTEPTASSMTSSSPISAWRWPTDGKVIENF-------SSSEGGNKGIDIAGSKGQAIIATADGRVVYAGN 300
Cdd:COG0739   44 ALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFgyrrhpvTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGW 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697053799 301 AlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS-TRLHFEIRYKGKSVNPLQYLPQ 373
Cdd:COG0739  124 N-GGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTgPHLHFEVRVNGKPVDPLPFLPA 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 272-367 4.20e-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: 139.99  E-value: 4.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  272 GGNKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 351
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 697053799  352 -TRLHFEIRYKGKSVNP 367
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 274-358 3.19e-30

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: 110.76  E-value: 3.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 274 NKGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS-T 352
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                 ....*.
gi 697053799 353 RLHFEI 358
Cdd:cd12797   80 HLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 232-373 4.89e-28

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: 108.96  E-value: 4.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 232 TAPVVSSTEPTASSMTSSSPISAWRWPTDGKVIENFS-----SSEGG----NKGIDIAGSKGQAIIATADGRVVYAGNAL 302
Cdd:COG5821   46 TVKNKSESNEKSKSKVTASTSNKFLKPVSGKITREFGedlvySKTLNewrtHTGIDIAAKEGTPVKAAADGVVVEVGKDP 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697053799 303 RgYGNLIIIKHNDDYLSAYAH-NDTMLVREQQEVKAGQKIATMGSTG--TSST--RLHFEIRYKGKSVNPLQYLPQ 373
Cdd:COG5821  126 K-YGITVVIDHGNGIKTVYANlDSKIKVKVGQKVKKGQVIGKVGSTAlfESSEgpHLHFEVLKNGKPVDPMKYLKK 200
PRK11637 PRK11637
AmiB activator; Provisional
 257-371 6.68e-22

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 96.30  E-value: 6.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 257 WPTDGKVIENFSSSEGGN---KGIDIAGSKGQAIIATADGRVVYAgNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQ 333
Cdd:PRK11637 309 WPVRGPTLHRFGEQLQGElrwKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGA 387

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 697053799 334 EVKAGQKIATMGSTGTSST-RLHFEIRYKGKSVNPLQYL 371
Cdd:PRK11637 388 QVRAGQPIALVGSSGGQGRpSLYFEIRRQGQAVNPQPWL 426
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 258-372 1.09e-19

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 86.58  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 258 PTDGKVIENFSSSeggNKGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKA 337
Cdd:COG5833  107 PVSGKVVESFQEN---GKGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEA 182

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 697053799 338 GQKIATMGSTGTSSTRLHFEIRYKGKSVNPLQYLP 372
Cdd:COG5833  183 GQKIGTVPATEGEEGTFYFAIKKGGKFIDPIQVIS 217
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 274-373 2.00e-15

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: 74.57  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 274 NKGIDIAGSKGQA--IIATADGRVVYAGN-ALrgYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGST--- 347
Cdd:COG5820  120 STGIDIAAKDGESfdVLAALSGTVTEVEEdPL--LGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGTAGRNlfn 197

                         90       100
                 ....*....|....*....|....*.
gi 697053799 348 GTSSTRLHFEIRYKGKSVNPLQYLPQ 373
Cdd:COG5820  198 KDAGVHLHFEVRKDGKAVNPESYLPK 223
PRK11649 PRK11649
putative peptidase; Provisional
 275-368 7.36e-14

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 72.39  E-value: 7.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799 275 KGIDIAGSKGQAIIATADGRVV---YAGNAlrgyGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 351
Cdd:PRK11649 314 RGVDFAMPVGTPVLAVGDGEVVvakRSGAA----GNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRST 389

                         90
                 ....*....|....*...
gi 697053799 352 -TRLHFEIRYKGKSVNPL 368
Cdd:PRK11649 390 gPHLHYEVWINQQAVNPL 407
LysM smart00257
Lysin motif;
117-160 2.32e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.45  E-value: 2.32e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 697053799   117 TYTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPYGLEVGQTLQV 160
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 118-160 1.24e-08

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: 50.47  E-value: 1.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 697053799  118 YTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPYgLEVGQTLQV 160
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 117-160 6.45e-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: 48.25  E-value: 6.45e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 697053799 117 TYTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPYGLEVGQTLQV 160
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 109-175 6.83e-06

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 47.81  E-value: 6.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697053799 109 KGSYTGGSTYTVKRGDTLFYIAWITGNDFRDLAQRNNVQAPyGLEVGQTLQVGNATGTPLTPGNTVS 175
Cdd:PRK10783 337 DNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGS-KLKVGQTLTIGAGSSAQRLANNSDS 402
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
53-160 7.50e-06

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 45.47  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  53 LITPPPKMGTSTAQQNPPIQPVQRPMTQPTQIQPVEQPVQTQNGRIVYNRQYGNIPKGSYTggsTYTVKRGDTLFYIAWI 132
Cdd:COG1388   50 AALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPV---TYTVKKGDTLWSIARR 126

                         90       100
                 ....*....|....*....|....*...
gi 697053799 133 TGNDFRDLAQRNNVqAPYGLEVGQTLQV 160
Cdd:COG1388  127 YGVSVEELKRWNGL-SSDTIRPGQKLKI 153
PRK00566 PRK00566
DNA-directed RNA polymerase subunit beta'; Provisional
 276-341 2.12e-03

DNA-directed RNA polymerase subunit beta'; Provisional


Pssm-ID: 234794 [Multi-domain]  Cd Length: 1156  Bit Score: 40.05  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  276 GIDIAGS-------------KGQAIIATADGRVVYaGNALRGYGNLIIIKHNDD---YL-SAYAHndtMLVREQQEVKAG 338
Cdd:PRK00566  906 GVDITGGlprvaelfearkpKGPAIIAEIDGTVSF-GKETKGKRRIVITPDDGEereYLiPKGKH---LLVQEGDHVEAG 981


                  ...
gi 697053799  339 QKI 341
Cdd:PRK00566  982 DKL 984
PRK06148 PRK06148
hypothetical protein; Provisional
 276-358 2.47e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 40.01  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053799  276 GIDIAGSKGQAIIATADGRVVYAGN-ALR-GYGNLIIIKHN----DDYLSAYAHNDTMLV---REQQEVKAGQKIATMGS 346
Cdd:PRK06148  443 GVDLFAPAGTPVYAPLAGTVRSVEIeAVPlGYGGLVALEHEtpggDPFYTLYGHLAHEAVsrlKPGDRLAAGELFGAMGD 522

                          90
                  ....*....|....*
gi 697053799  347 TGTSSTR---LHFEI 358
Cdd:PRK06148  523 AHENGGWaphLHFQL 537
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH