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Conserved domains on  [gi|535277498|gb|EQU20663|]
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lipoprotein YgeR [Escherichia coli HVH 201 (4-4459431)]

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

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List of domain hits

 Name Accession Description Interval E-value
amid_act_ActS NF040883
amidase activator ActS;
7-251 8.44e-174

amidase activator ActS;


:

Pssm-ID: 468819 [Multi-domain]  Cd Length: 242  Bit Score: 478.10  E-value: 8.44e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498   7 NKKSLGIVMLLSVGLLLAGCSGSKSSDTGTYSGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPYTIEVGQKLKLGG 86
Cdd:NF040883   1 LALWFRIAVCLTLGLLLAGCSGKKSDYDGSYSGSTYTVKRGDTLYRISRITGTSVSELARLNGISPPYTIEVGQKLRLNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  87 AKSSSSTRKstaKSTTKTASVTPSSAVPKSSWPPVGQRCWLWPTTGKVIMPYSTADGGNKGIDISAPRGTPIYAAGAGKV 166
Cdd:NF040883  81 SSKSKKSAA---KSSTKTAKVTPSSAVPKSSWPPVGQRCWRWPTSGKVVLPYSTADGGNKGIDIAGKRGQPVYASGAGKV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 167 VYVGNQLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAASVRLHFQIRYRATAIDPLRYLPPQG 246
Cdd:NF040883 158 VYVGNQLRGYGNLIMIKHGEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTGADSVRLHFQIRYRATAIDPLRYLPPQG 237


                 ....*
gi 535277498 247 SKPKC 251
Cdd:NF040883 238 SKPSC 242
 
Name Accession Description Interval E-value
amid_act_ActS NF040883
amidase activator ActS;
7-251 8.44e-174

amidase activator ActS;


Pssm-ID: 468819 [Multi-domain]  Cd Length: 242  Bit Score: 478.10  E-value: 8.44e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498   7 NKKSLGIVMLLSVGLLLAGCSGSKSSDTGTYSGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPYTIEVGQKLKLGG 86
Cdd:NF040883   1 LALWFRIAVCLTLGLLLAGCSGKKSDYDGSYSGSTYTVKRGDTLYRISRITGTSVSELARLNGISPPYTIEVGQKLRLNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  87 AKSSSSTRKstaKSTTKTASVTPSSAVPKSSWPPVGQRCWLWPTTGKVIMPYSTADGGNKGIDISAPRGTPIYAAGAGKV 166
Cdd:NF040883  81 SSKSKKSAA---KSSTKTAKVTPSSAVPKSSWPPVGQRCWRWPTSGKVVLPYSTADGGNKGIDIAGKRGQPVYASGAGKV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 167 VYVGNQLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAASVRLHFQIRYRATAIDPLRYLPPQG 246
Cdd:NF040883 158 VYVGNQLRGYGNLIMIKHGEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTGADSVRLHFQIRYRATAIDPLRYLPPQG 237


                 ....*
gi 535277498 247 SKPKC 251
Cdd:NF040883 238 SKPSC 242
nlpD PRK10871
murein hydrolase activator NlpD;
1-243 3.46e-77

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 235.89  E-value: 3.46e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498   1 MSAGRLNKKSLGIVMLLSVGLLLAGCSGSKSSDT---------------------GTYSGSVYTVKRGDTLYRISRTTGT 59
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPApvssvgngrivynrqygnipkGSYSGSTYTVKKGDTLFYIAWITGN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  60 SVKELARLNGISPPYTIEVGQKLKLGGAK--------------------------------------------------- 88
Cdd:PRK10871  81 DFRDLAQRNNIQAPYSLNVGQTLQVGNASgtpitggnaitqadaaeqgvvikpaqnstvavasqptitysessgeqsank 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  89 ----SSSSTRKSTAKSTTKTASVTPSSAVPKSSWPPVGQrcWLWPTTGKVIMPYSTADGGNKGIDISAPRGTPIYAAGAG 164
Cdd:PRK10871 161 mlpnNKPAATTVTAPVTAPTASTTEPTASSTSTSTPIST--WRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADG 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535277498 165 KVVYVGNQLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAASVRLHFQIRYRATAIDPLRYLP 243
Cdd:PRK10871 239 RVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLP 317
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 126-245 8.15e-49

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: 164.94  E-value: 8.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 126 WLWPTTGKVIMPYSTADGG---NKGIDISAPRGTPIYAAGAGKVVYVGNqLRGYGNLIMIKHSEDYITAYAHNDTMLVNN 202
Cdd:COG4942  255 LPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLSSLLVKV 333

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 535277498 203 GQSVKAGQKIATMGSTDAAS-VRLHFQIRYRATAIDPLRYLPPQ 245
Cdd:COG4942  334 GQRVKAGQPIGTVGSSGGQGgPTLYFELRKNGKPVDPLPWLAKR 377
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 143-238 1.22e-40

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: 134.98  E-value: 1.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  143 GGNKGIDISAPRGTPIYAAGAGKVVYVGNqLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAAS 222
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 535277498  223 -VRLHFQIRYRATAIDP 238
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 145-229 1.63e-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: 111.14  E-value: 1.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 145 NKGIDISAPRGTPIYAAGAGKVVYVGNQlRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAAS-V 223
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                 ....*.
gi 535277498 224 RLHFQI 229
Cdd:cd12797   80 HLHFEI 85
LysM smart00257
Lysin motif;
42-84 5.46e-14

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 64.39  E-value: 5.46e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 535277498    42 YTVKRGDTLYRISRTTGTSVKELARLNGISPPYTIEVGQKLKL 84
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
amid_act_ActS NF040883
amidase activator ActS;
7-251 8.44e-174

amidase activator ActS;


Pssm-ID: 468819 [Multi-domain]  Cd Length: 242  Bit Score: 478.10  E-value: 8.44e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498   7 NKKSLGIVMLLSVGLLLAGCSGSKSSDTGTYSGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPYTIEVGQKLKLGG 86
Cdd:NF040883   1 LALWFRIAVCLTLGLLLAGCSGKKSDYDGSYSGSTYTVKRGDTLYRISRITGTSVSELARLNGISPPYTIEVGQKLRLNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  87 AKSSSSTRKstaKSTTKTASVTPSSAVPKSSWPPVGQRCWLWPTTGKVIMPYSTADGGNKGIDISAPRGTPIYAAGAGKV 166
Cdd:NF040883  81 SSKSKKSAA---KSSTKTAKVTPSSAVPKSSWPPVGQRCWRWPTSGKVVLPYSTADGGNKGIDIAGKRGQPVYASGAGKV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 167 VYVGNQLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAASVRLHFQIRYRATAIDPLRYLPPQG 246
Cdd:NF040883 158 VYVGNQLRGYGNLIMIKHGEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTGADSVRLHFQIRYRATAIDPLRYLPPQG 237


                 ....*
gi 535277498 247 SKPKC 251
Cdd:NF040883 238 SKPSC 242
nlpD PRK10871
murein hydrolase activator NlpD;
1-243 3.46e-77

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 235.89  E-value: 3.46e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498   1 MSAGRLNKKSLGIVMLLSVGLLLAGCSGSKSSDT---------------------GTYSGSVYTVKRGDTLYRISRTTGT 59
Cdd:PRK10871   1 MSAGSPKFTVRRIAALSLVSLWLAGCSNTSNPPApvssvgngrivynrqygnipkGSYSGSTYTVKKGDTLFYIAWITGN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  60 SVKELARLNGISPPYTIEVGQKLKLGGAK--------------------------------------------------- 88
Cdd:PRK10871  81 DFRDLAQRNNIQAPYSLNVGQTLQVGNASgtpitggnaitqadaaeqgvvikpaqnstvavasqptitysessgeqsank 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  89 ----SSSSTRKSTAKSTTKTASVTPSSAVPKSSWPPVGQrcWLWPTTGKVIMPYSTADGGNKGIDISAPRGTPIYAAGAG 164
Cdd:PRK10871 161 mlpnNKPAATTVTAPVTAPTASTTEPTASSTSTSTPIST--WRWPTDGKVIENFSASEGGNKGIDIAGSKGQAIIATADG 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535277498 165 KVVYVGNQLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAASVRLHFQIRYRATAIDPLRYLP 243
Cdd:PRK10871 239 RVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLP 317
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 126-245 8.15e-49

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: 164.94  E-value: 8.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 126 WLWPTTGKVIMPYSTADGG---NKGIDISAPRGTPIYAAGAGKVVYVGNqLRGYGNLIMIKHSEDYITAYAHNDTMLVNN 202
Cdd:COG4942  255 LPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYAGW-LRGYGNLVIIDHGGGYLTLYAHLSSLLVKV 333

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 535277498 203 GQSVKAGQKIATMGSTDAAS-VRLHFQIRYRATAIDPLRYLPPQ 245
Cdd:COG4942  334 GQRVKAGQPIGTVGSSGGQGgPTLYFELRKNGKPVDPLPWLAKR 377
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 128-244 3.60e-46

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: 152.82  E-value: 3.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 128 WPTTGKVIMPY-------STADGGNKGIDISAPRGTPIYAAGAGKVVYVGNQlRGYGNLIMIKHSEDYITAYAHNDTMLV 200
Cdd:COG0739   73 WPVKGRITSGFgyrrhpvTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWN-GGYGNLVIIDHGNGYTTLYAHLSSILV 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 535277498 201 NNGQSVKAGQKIATMGSTDAAS-VRLHFQIRYRATAIDPLRYLPP 244
Cdd:COG0739  152 KVGQRVKAGQVIGYVGNTGRSTgPHLHFEVRVNGKPVDPLPFLPA 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 143-238 1.22e-40

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: 134.98  E-value: 1.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  143 GGNKGIDISAPRGTPIYAAGAGKVVYVGNqLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAAS 222
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 535277498  223 -VRLHFQIRYRATAIDP 238
Cdd:pfam01551  80 gPHLHFEIRKNGKPVDP 96
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 99-244 7.86e-32

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: 115.89  E-value: 7.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  99 KSTTKTASVTPSSAVPKSSWPPVgqrcWLWPTTGKVIMPYS-------TADG--GNKGIDISAPRGTPIYAAGAGKVVYV 169
Cdd:COG5821   46 TVKNKSESNEKSKSKVTASTSNK----FLKPVSGKITREFGedlvyskTLNEwrTHTGIDIAAKEGTPVKAAADGVVVEV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 170 GNQLRgYGNLIMIKHSEDYITAYAH-NDTMLVNNGQSVKAGQKIATMGST----DAASVRLHFQIRYRATAIDPLRYLPP 244
Cdd:COG5821  122 GKDPK-YGITVVIDHGNGIKTVYANlDSKIKVKVGQKVKKGQVIGKVGSTalfeSSEGPHLHFEVLKNGKPVDPMKYLKK 200
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 145-229 1.63e-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: 111.14  E-value: 1.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 145 NKGIDISAPRGTPIYAAGAGKVVYVGNQlRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKAGQKIATMGSTDAAS-V 223
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTgP 79


                 ....*.
gi 535277498 224 RLHFQI 229
Cdd:cd12797   80 HLHFEI 85
PRK11637 PRK11637
AmiB activator; Provisional
 120-242 8.25e-18

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 81.66  E-value: 8.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 120 PVGQRcwLWPTTGKVIMPYSTADGGN---KGIDISAPRGTPIYAAGAGKVVyVGNQLRGYGNLIMIKHSEDYITAYAHND 196
Cdd:PRK11637 303 PRGQA--FWPVRGPTLHRFGEQLQGElrwKGMVIGASEGTEVKAIADGRVL-LADWLQGYGLVVVVEHGKGDMSLYGYNQ 379

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 535277498 197 TMLVNNGQSVKAGQKIATMGSTDAASV-RLHFQIRYRATAIDPLRYL 242
Cdd:PRK11637 380 SALVSVGAQVRAGQPIALVGSSGGQGRpSLYFEIRRQGQAVNPQPWL 426
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 126-243 6.80e-17

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 76.57  E-value: 6.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 126 WLWPTTGKVIMPYstADGGnKGIDISAPRGTPIYAAGAGKVVYVGNQlRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQS 205
Cdd:COG5833  104 FALPVSGKVVESF--QENG-KGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVIIQHADGSESWYGNLSSIDVKLYDF 179

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 535277498 206 VKAGQKIATMGSTDAASVRLHFQIRYRATAIDPLRYLP 243
Cdd:COG5833  180 VEAGQKIGTVPATEGEEGTFYFAIKKGGKFIDPIQVIS 217
PRK11649 PRK11649
putative peptidase; Provisional
 129-239 7.86e-16

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 76.24  E-value: 7.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498 129 PTTGKvIMPYstadggnKGIDISAPRGTPIYAAGAGKVVyVGNQLRGYGNLIMIKHSEDYITAYAHNDTMLVNNGQSVKA 208
Cdd:PRK11649 305 PVTGR-VAPH-------RGVDFAMPVGTPVLAVGDGEVV-VAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKR 375

                         90       100       110
                 ....*....|....*....|....*....|..
gi 535277498 209 GQKIATMGSTDAAS-VRLHFQIRYRATAIDPL 239
Cdd:PRK11649 376 GDRIALSGNTGRSTgPHLHYEVWINQQAVNPL 407
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 41-84 1.96e-14

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: 65.58  E-value: 1.96e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 535277498  41 VYTVKRGDTLYRISRTTGTSVKELARLNGISPPYTIEVGQKLKL 84
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 42-84 4.89e-14

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: 64.34  E-value: 4.89e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 535277498   42 YTVKRGDTLYRISRTTGTSVKELARLNGISPPyTIEVGQKLKL 84
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSP-NLYVGQKLKI 42
LysM smart00257
Lysin motif;
42-84 5.46e-14

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 64.39  E-value: 5.46e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 535277498    42 YTVKRGDTLYRISRTTGTSVKELARLNGISPPYTIEVGQKLKL 84
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
29-84 2.64e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.89  E-value: 2.64e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 535277498  29 SKSSDTGTYSGSVYTVKRGDTLYRISRTTGTSVKELARLNGISpPYTIEVGQKLKL 84
Cdd:COG1388   99 RRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLS-SDTIRPGQKLKI 153
PRK06148 PRK06148
hypothetical protein; Provisional
 147-229 9.07e-10

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 58.50  E-value: 9.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  147 GIDISAPRGTPIYAAGAGKVVYVGNQLR--GYGNLIMIKHS----EDYITAYAHNDTMLVNN---GQSVKAGQKIATMGS 217
Cdd:PRK06148  443 GVDLFAPAGTPVYAPLAGTVRSVEIEAVplGYGGLVALEHEtpggDPFYTLYGHLAHEAVSRlkpGDRLAAGELFGAMGD 522

                          90
                  ....*....|....*
gi 535277498  218 TDAASVR---LHFQI 229
Cdd:PRK06148  523 AHENGGWaphLHFQL 537
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 12-84 5.97e-08

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: 51.16  E-value: 5.97e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535277498  12 GIVMLLSVGLLLAGCSGSKSSDTGTYSGSVYTVKRGDTLYRISRT---TGTSVKELARLN--GISPPYTIEVGQKLKL 84
Cdd:COG1652   82 GAAAKLSPAVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRfygDPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 38-85 4.41e-06

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 47.04  E-value: 4.41e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 535277498  38 SGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPyTIEVGQKLKLG 85
Cdd:PRK10783 342 NSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGS-KLKVGQTLTIG 388
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
25-126 2.04e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 45.07  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  25 GCSGSKSSDTGTYSGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPyTIEVGQKLKLGGAKSSSSTrkstakSTTKT 104
Cdd:PRK06347 465 NTNTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSD-FIYPGQKLKVSAGSTTNNT------NTAKP 537

                         90       100
                 ....*....|....*....|..
gi 535277498 105 ASVTPSSAVPKSSWPPVGQRCW 126
Cdd:PRK06347 538 STNKPSNSTVKTYTVKKGDSLW 559
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
24-134 2.28e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 45.07  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  24 AGCSGSKSSDTGTYSGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPYtIEVGQKLKLGGAKSSSSTRKSTAKSTTK 103
Cdd:PRK06347 315 TGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDF-IYPGQKLKVSAGSTTSDTNTSKPSTGTS 393

                         90       100       110
                 ....*....|....*....|....*....|..
gi 535277498 104 TASVTPSSAVPKSSWPPV-GQRCWLWPTTGKV 134
Cdd:PRK06347 394 TSKPSTGTSTNAKVYTVVkGDSLWRIANNNKV 425
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
25-111 7.38e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 43.53  E-value: 7.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  25 GCSGSKSSDTGTYSGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPYtIEVGQKLKLggaKSSSSTRKSTAKSTTKT 104
Cdd:PRK06347 391 GTSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDF-IYPGQKLKV---SAGSTSNTNTSKPSTNT 466


                 ....*..
gi 535277498 105 ASVTPSS 111
Cdd:PRK06347 467 NTSKPST 473
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
27-84 1.50e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 39.68  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 535277498  27 SGSKSSDTGTysgSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPyTIEVGQKLKL 84
Cdd:PRK06347 538 STNKPSNSTV---KTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSN-MIHVGQKLTI 591
PRK13914 PRK13914
invasion associated endopeptidase;
38-121 5.56e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 37.86  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277498  38 SGSVYTVKRGDTLYRISRTTGTSVKELARLNGISPPyTIEVGQKLKLggaksssstrKSTAKSTTKTASV-TPSSAVPKS 116
Cdd:PRK13914 198 NATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSS-SIYVGQKLAI----------KQTANTATPKAEVkTEAPAAEKQ 266


                 ....*
gi 535277498 117 SWPPV 121
Cdd:PRK13914 267 AAPVV 271
 
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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