NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490364672|ref|WP_004244344|]
View 

MULTISPECIES: murein hydrolase activator NlpD [Proteus]

Protein Classification

M23 peptidase family protein( domain architecture ID 1000974)

M23 peptidase family protein similar to murein hydrolase activator NlpD and to Haemophilus somni LppB lipoprotein outer membrane antigen, a putative virulence determinant; NlpD/LppB contains LysM and M23 peptidase domains

Gene Ontology:  GO:0004222|GO:0009279
MEROPS:  M23
PubMed:  19759820|8478068

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 super family cl35964
murein hydrolase activator NlpD;
1-374 7.08e-116

murein hydrolase activator NlpD;


The actual alignment was detected with superfamily member PRK10871:

Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 339.50  E-value: 7.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672   1 MNSESPIKHVRWAIMCSVIGFALTGCADTPYRPAPITSVndsssnrtvstspvttnsnagvatpiergstplqttpppsi 80
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPAPVSSV----------------------------------------- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672  81 rvnnttaqpqsqprtqnvtpqnvntdGSGRIVYNRNYDNIPKGNYSGNTYTVKRGDTMFYIAWITDSDVKDLASMNNIPE 160
Cdd:PRK10871  40 --------------------------GNGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQA 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 161 PYSLNVGQVLKIGNRQVNTGT-------NTNVNTSVINKPSSEGVQTAQTKPSNNNS------SMGPLITKPTTTTPPKT 227
Cdd:PRK10871  94 PYSLNVGQTLQVGNASGTPITggnaitqADAAEQGVVIKPAQNSTVAVASQPTITYSessgeqSANKMLPNNKPAATTVT 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 228 TTSTPTTSATTSNNTTATSKPAAATGkWVWPAQGKIIESYSNAPGGNKGIDISGTRGSPIVATAAGKVVYAGSALRGYGN 307
Cdd:PRK10871 174 APVTAPTASTTEPTASSTSTSTPIST-WRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGN 252

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490364672 308 LVIIKHNDEYLSAYAHNDTILVREQQNVNAGQQIATMGSTGTSSVRLHFEIRYKEKSLNPMSYLPKR 374
Cdd:PRK10871 253 LIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
1-374 7.08e-116

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 339.50  E-value: 7.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672   1 MNSESPIKHVRWAIMCSVIGFALTGCADTPYRPAPITSVndsssnrtvstspvttnsnagvatpiergstplqttpppsi 80
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPAPVSSV----------------------------------------- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672  81 rvnnttaqpqsqprtqnvtpqnvntdGSGRIVYNRNYDNIPKGNYSGNTYTVKRGDTMFYIAWITDSDVKDLASMNNIPE 160
Cdd:PRK10871  40 --------------------------GNGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQA 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 161 PYSLNVGQVLKIGNRQVNTGT-------NTNVNTSVINKPSSEGVQTAQTKPSNNNS------SMGPLITKPTTTTPPKT 227
Cdd:PRK10871  94 PYSLNVGQTLQVGNASGTPITggnaitqADAAEQGVVIKPAQNSTVAVASQPTITYSessgeqSANKMLPNNKPAATTVT 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 228 TTSTPTTSATTSNNTTATSKPAAATGkWVWPAQGKIIESYSNAPGGNKGIDISGTRGSPIVATAAGKVVYAGSALRGYGN 307
Cdd:PRK10871 174 APVTAPTASTTEPTASSTSTSTPIST-WRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGN 252

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490364672 308 LVIIKHNDEYLSAYAHNDTILVREQQNVNAGQQIATMGSTGTSSVRLHFEIRYKEKSLNPMSYLPKR 374
Cdd:PRK10871 253 LIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 249-374 1.10e-51

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: 176.49  E-value: 1.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 249 AAATGKWVWPAQGKIIESYSNAPGG---NKGIDISGTRGSPIVATAAGKVVYAGSaLRGYGNLVIIKHNDEYLSAYAHND 325
Cdd:COG4942  249 AALKGKLPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLS 327

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490364672 326 TILVREQQNVNAGQQIATMGSTG-TSSVRLHFEIRYKEKSLNPMSYLPKR 374
Cdd:COG4942  328 SLLVKVGQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGKPVDPLPWLAKR 377
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 272-367 2.06e-39

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: 135.37  E-value: 2.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672  272 GGNKGIDISGTRGSPIVATAAGKVVYAGSaLRGYGNLVIIKHNDEYLSAYAHNDTILVREQQNVNAGQQIATMGSTGTSS 351
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 490364672  352 -VRLHFEIRYKEKSLNP 367
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 274-358 5.01e-31

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: 113.07  E-value: 5.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 274 NKGIDISGTRGSPIVATAAGKVVYAGSAlRGYGNLVIIKHNDEYLSAYAHNDTILVREQQNVNAGQQIATMGSTGTSS-V 352
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                 ....*.
gi 490364672 353 RLHFEI 358
Cdd:cd12797   80 HLHFEI 85
LysM smart00257
Lysin motif;
129-172 1.39e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 55.91  E-value: 1.39e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 490364672   129 TYTVKRGDTMFYIAWITDSDVKDLASMNNIPEPYSLNVGQVLKI 172
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
1-374 7.08e-116

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 339.50  E-value: 7.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672   1 MNSESPIKHVRWAIMCSVIGFALTGCADTPYRPAPITSVndsssnrtvstspvttnsnagvatpiergstplqttpppsi 80
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPAPVSSV----------------------------------------- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672  81 rvnnttaqpqsqprtqnvtpqnvntdGSGRIVYNRNYDNIPKGNYSGNTYTVKRGDTMFYIAWITDSDVKDLASMNNIPE 160
Cdd:PRK10871  40 --------------------------GNGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQA 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 161 PYSLNVGQVLKIGNRQVNTGT-------NTNVNTSVINKPSSEGVQTAQTKPSNNNS------SMGPLITKPTTTTPPKT 227
Cdd:PRK10871  94 PYSLNVGQTLQVGNASGTPITggnaitqADAAEQGVVIKPAQNSTVAVASQPTITYSessgeqSANKMLPNNKPAATTVT 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 228 TTSTPTTSATTSNNTTATSKPAAATGkWVWPAQGKIIESYSNAPGGNKGIDISGTRGSPIVATAAGKVVYAGSALRGYGN 307
Cdd:PRK10871 174 APVTAPTASTTEPTASSTSTSTPIST-WRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGN 252

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490364672 308 LVIIKHNDEYLSAYAHNDTILVREQQNVNAGQQIATMGSTGTSSVRLHFEIRYKEKSLNPMSYLPKR 374
Cdd:PRK10871 253 LIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR 319
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 249-374 1.10e-51

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: 176.49  E-value: 1.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 249 AAATGKWVWPAQGKIIESYSNAPGG---NKGIDISGTRGSPIVATAAGKVVYAGSaLRGYGNLVIIKHNDEYLSAYAHND 325
Cdd:COG4942  249 AALKGKLPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLS 327

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490364672 326 TILVREQQNVNAGQQIATMGSTG-TSSVRLHFEIRYKEKSLNPMSYLPKR 374
Cdd:COG4942  328 SLLVKVGQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGKPVDPLPWLAKR 377
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 248-373 5.30e-45

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: 153.59  E-value: 5.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 248 PAAATGKWVWPAQGKIIESY-------SNAPGGNKGIDISGTRGSPIVATAAGKVVYAGSAlRGYGNLVIIKHNDEYLSA 320
Cdd:COG0739   64 AAIALGSGAWPVKGRITSGFgyrrhpvTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWN-GGYGNLVIIDHGNGYTTL 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490364672 321 YAHNDTILVREQQNVNAGQQIATMGSTGTSS-VRLHFEIRYKEKSLNPMSYLPK 373
Cdd:COG0739  143 YAHLSSILVKVGQRVKAGQVIGYVGNTGRSTgPHLHFEVRVNGKPVDPLPFLPA 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 272-367 2.06e-39

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: 135.37  E-value: 2.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672  272 GGNKGIDISGTRGSPIVATAAGKVVYAGSaLRGYGNLVIIKHNDEYLSAYAHNDTILVREQQNVNAGQQIATMGSTGTSS 351
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 490364672  352 -VRLHFEIRYKEKSLNP 367
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 274-358 5.01e-31

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: 113.07  E-value: 5.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 274 NKGIDISGTRGSPIVATAAGKVVYAGSAlRGYGNLVIIKHNDEYLSAYAHNDTILVREQQNVNAGQQIATMGSTGTSS-V 352
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                 ....*.
gi 490364672 353 RLHFEI 358
Cdd:cd12797   80 HLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 249-373 5.21e-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: 108.57  E-value: 5.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 249 AAATGKWVWPAQGKIIESYSNAPG---------GNKGIDISGTRGSPIVATAAGKVVYAGSALRgYGNLVIIKHNDEYLS 319
Cdd:COG5821   63 ASTSNKFLKPVSGKITREFGEDLVysktlnewrTHTGIDIAAKEGTPVKAAADGVVVEVGKDPK-YGITVVIDHGNGIKT 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490364672 320 AYAH-NDTILVREQQNVNAGQQIATMGSTGTSSV----RLHFEIRYKEKSLNPMSYLPK 373
Cdd:COG5821  142 VYANlDSKIKVKVGQKVKKGQVIGKVGSTALFESsegpHLHFEVLKNGKPVDPMKYLKK 200
PRK11637 PRK11637
AmiB activator; Provisional
 247-371 2.66e-18

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 85.90  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 247 KPAaatGKWVWPAQGKIIESYSNAPGGN---KGIDISGTRGSPIVATAAGKVVYAgSALRGYGNLVIIKHNDEYLSAYAH 323
Cdd:PRK11637 302 RPR---GQAFWPVRGPTLHRFGEQLQGElrwKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMSLYGY 377

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490364672 324 NDTILVREQQNVNAGQQIATMGSTG---TSSvrLHFEIRYKEKSLNPMSYL 371
Cdd:PRK11637 378 NQSALVSVGAQVRAGQPIALVGSSGgqgRPS--LYFEIRRQGQAVNPQPWL 426
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 255-372 1.05e-15

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 75.41  E-value: 1.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 255 WVWPAQGKIIESYSNapgGNKGIDISGTRGSPIVATAAGKVVYAGSAlRGYGNLVIIKHNDEYLSAYAHNDTILVREQQN 334
Cdd:COG5833  104 FALPVSGKVVESFQE---NGKGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVIIQHADGSESWYGNLSSIDVKLYDF 179

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490364672 335 VNAGQQIATMGSTGTSSVRLHFEIRYKEKSLNPMSYLP 372
Cdd:COG5833  180 VEAGQKIGTVPATEGEEGTFYFAIKKGGKFIDPIQVIS 217
PRK11649 PRK11649
putative peptidase; Provisional
 258-369 3.64e-12

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 67.38  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672 258 PAQGKIiesysnAPggNKGIDISGTRGSPIVATAAGKVV---YAGSAlrgyGNLVIIKHNDEYLSAYAHNDTILVREQQN 334
Cdd:PRK11649 305 PVTGRV------AP--HRGVDFAMPVGTPVLAVGDGEVVvakRSGAA----GNYVAIRHGRQYTTRYMHLRKLLVKPGQK 372

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490364672 335 VNAGQQIATMGSTGTSS-VRLHFEIRYKEKSLNPMS 369
Cdd:PRK11649 373 VKRGDRIALSGNTGRSTgPHLHYEVWINQQAVNPLT 408
LysM smart00257
Lysin motif;
129-172 1.39e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 55.91  E-value: 1.39e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 490364672   129 TYTVKRGDTMFYIAWITDSDVKDLASMNNIPEPYSLNVGQVLKI 172
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 ...
 130-172 1.84e-09

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: 52.78  E-value: 1.84e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 490364672  130 YTVKRGDTMFYIAWITDSDVKDLASMNNIPEPYsLNVGQVLKI 172
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 129-172 3.87e-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: 51.72  E-value: 3.87e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490364672 129 TYTVKRGDTMFYIAWITDSDVKDLASMNNIPEPYSLNVGQVLKI 172
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
27-172 1.35e-07

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 50.86  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672  27 ADTPYRPAPITSVNDSSSNRTVSTSPVTTNSNAGVATPIERGSTPLQTTPPPSIRVNNTTAQPQSQPRTQNVTPQNVNTD 106
Cdd:COG1388   11 ALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKS 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490364672 107 GSGRIVYNRNYDNIPKGNYSgnTYTVKRGDTMFYIAWITDSDVKDLASMNNIpEPYSLNVGQVLKI 172
Cdd:COG1388   91 GDTLSGIARRYGAAAAPSPV--TYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKI 153
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 126-174 2.63e-03

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 39.72  E-value: 2.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490364672 126 SGNTYTVKRGDTMFYIAWITDSDVKDLASMNNIpEPYSLNVGQVLKIGN 174
Cdd:PRK10783 342 NSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNL-RGSKLKVGQTLTIGA 389
PRK06148 PRK06148
hypothetical protein; Provisional
 276-358 2.91e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 39.62  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364672  276 GIDISGTRGSPIVATAAGKVV-YAGSALR-GYGNLVIIKHN----DEYLSAYAHNDTILV---REQQNVNAGQQIATMGS 346
Cdd:PRK06148  443 GVDLFAPAGTPVYAPLAGTVRsVEIEAVPlGYGGLVALEHEtpggDPFYTLYGHLAHEAVsrlKPGDRLAAGELFGAMGD 522

                          90
                  ....*....|....*
gi 490364672  347 TGTSSVR---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