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Conserved domains on  [gi|15600117|ref|NP_253611|]
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hypothetical protein PA4924 [Pseudomonas aeruginosa PAO1]

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
nlpD super family cl35964
murein hydrolase activator NlpD;
36-220 1.16e-44

murein hydrolase activator NlpD;


The actual alignment was detected with superfamily member PRK10871:

Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 151.91  E-value: 1.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   36 YRVKRGDTLYSIATRHGWNYKDLARANGIRPPYAVKVGQVVRFDG----------------------------RKSTYVA 87
Cdd:PRK10871  63 YTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNasgtpitggnaitqadaaeqgvvikpaqNSTVAVA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   88 S------SRSSSNTRARK---------------------------PPPPPPSVTLRGWQWPMKGPVIRRFSSSDKLNKGI 134
Cdd:PRK10871 143 SqptitySESSGEQSANKmlpnnkpaattvtapvtaptastteptASSTSTSTPISTWRWPTDGKVIENFSASEGGNKGI 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  135 RIAGTLGQPVQASLAGKVVFAVNNMRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSSDADRVQLYFE 214
Cdd:PRK10871 223 DIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFE 302


                 ....*.
gi 15600117  215 IRQNGR 220
Cdd:PRK10871 303 IRYKGK 308
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
36-220 1.16e-44

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 151.91  E-value: 1.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   36 YRVKRGDTLYSIATRHGWNYKDLARANGIRPPYAVKVGQVVRFDG----------------------------RKSTYVA 87
Cdd:PRK10871  63 YTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNasgtpitggnaitqadaaeqgvvikpaqNSTVAVA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   88 S------SRSSSNTRARK---------------------------PPPPPPSVTLRGWQWPMKGPVIRRFSSSDKLNKGI 134
Cdd:PRK10871 143 SqptitySESSGEQSANKmlpnnkpaattvtapvtaptastteptASSTSTSTPISTWRWPTDGKVIENFSASEGGNKGI 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  135 RIAGTLGQPVQASLAGKVVFAVNNMRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSSDADRVQLYFE 214
Cdd:PRK10871 223 DIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFE 302


                 ....*.
gi 15600117  215 IRQNGR 220
Cdd:PRK10871 303 IRYKGK 308
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 96-220 2.33e-41

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: 144.52  E-value: 2.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  96 RARKPPPPPPSVTLRG-WQWPMKGPVIRRFSSSDKL---NKGIRIAGTLGQPVQASLAGKVVFAvNNMRGYGNLVIIQHG 171
Cdd:COG4942 238 AAAERTPAAGFAALKGkLPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYA-GWLRGYGNLVIIDHG 316

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15600117 172 TSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSSD-ADRVQLYFEIRQNGR 220
Cdd:COG4942 317 GGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGK 366
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 131-220 4.14e-32

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: 112.64  E-value: 4.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   131 NKGIRIAGTLGQPVQASLAGKVVFAvNNMRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSSD-ADRV 209
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFA-GWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGrSTGP 81

                          90
                  ....*....|.
gi 15600117   210 QLYFEIRQNGR 220
Cdd:pfam01551  82 HLHFEIRKNGK 92
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 131-215 2.54e-26

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: 97.28  E-value: 2.54e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117 131 NKGIRIAGTLGQPVQASLAGKVVFAVNNmRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSS-DADRV 209
Cdd:cd12797   1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTgRSTGP 79


                ....*.
gi 15600117 210 QLYFEI 215
Cdd:cd12797  80 HLHFEI 85
LysM smart00257
Lysin motif;
35-77 1.19e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.84  E-value: 1.19e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 15600117     35 EYRVKRGDTLYSIATRHGWNYKDLARANGIRPPYAVKVGQVVR 77
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLK 43
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
36-220 1.16e-44

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 151.91  E-value: 1.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   36 YRVKRGDTLYSIATRHGWNYKDLARANGIRPPYAVKVGQVVRFDG----------------------------RKSTYVA 87
Cdd:PRK10871  63 YTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNasgtpitggnaitqadaaeqgvvikpaqNSTVAVA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   88 S------SRSSSNTRARK---------------------------PPPPPPSVTLRGWQWPMKGPVIRRFSSSDKLNKGI 134
Cdd:PRK10871 143 SqptitySESSGEQSANKmlpnnkpaattvtapvtaptastteptASSTSTSTPISTWRWPTDGKVIENFSASEGGNKGI 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  135 RIAGTLGQPVQASLAGKVVFAVNNMRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSSDADRVQLYFE 214
Cdd:PRK10871 223 DIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFE 302


                 ....*.
gi 15600117  215 IRQNGR 220
Cdd:PRK10871 303 IRYKGK 308
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 96-220 2.33e-41

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: 144.52  E-value: 2.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  96 RARKPPPPPPSVTLRG-WQWPMKGPVIRRFSSSDKL---NKGIRIAGTLGQPVQASLAGKVVFAvNNMRGYGNLVIIQHG 171
Cdd:COG4942 238 AAAERTPAAGFAALKGkLPWPVSGRVVRRFGERDGGggrNKGIDIAAPPGAPVRAVADGTVVYA-GWLRGYGNLVIIDHG 316

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15600117 172 TSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSSD-ADRVQLYFEIRQNGR 220
Cdd:COG4942 317 GGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGgQGGPTLYFELRKNGK 366
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 39-220 2.05e-33

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: 119.31  E-value: 2.05e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  39 KRGDTLYSIATRHGWNYKDLARANGIRPPYAVKVGQVVRFDGRKSTYVASSRSSSNTRARkppPPPPSVTLRGWQWPMKG 118
Cdd:COG0739   1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAA---AAAAAIALGSGAWPVKG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117 119 PVIRRF-------SSSDKLNKGIRIAGTLGQPVQASLAGKVVFAVNNmRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQM 191
Cdd:COG0739  78 RITSGFgyrrhpvTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWN-GGYGNLVIIDHGNGYTTLYAHLSSILVKVGQR 156

                       170       180       190
                ....*....|....*....|....*....|
gi 15600117 192 VGKGQKIAEAGSSD-ADRVQLYFEIRQNGR 220
Cdd:COG0739 157 VKAGQVIGYVGNTGrSTGPHLHFEVRVNGK 186
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 131-220 4.14e-32

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: 112.64  E-value: 4.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   131 NKGIRIAGTLGQPVQASLAGKVVFAvNNMRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSSD-ADRV 209
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFA-GWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGrSTGP 81

                          90
                  ....*....|.
gi 15600117   210 QLYFEIRQNGR 220
Cdd:pfam01551  82 HLHFEIRKNGK 92
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 131-215 2.54e-26

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: 97.28  E-value: 2.54e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117 131 NKGIRIAGTLGQPVQASLAGKVVFAVNNmRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGKGQKIAEAGSS-DADRV 209
Cdd:cd12797   1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTgRSTGP 79


                ....*.
gi 15600117 210 QLYFEI 215
Cdd:cd12797  80 HLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 114-219 1.10e-25

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: 99.33  E-value: 1.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117 114 WPMKGPVIRRFSssDKL-----------NKGIRIAGTLGQPVQASLAGKVVFAVNNMRgYGNLVIIQHGTSYTSTYAH-N 181
Cdd:COG5821  71 KPVSGKITREFG--EDLvysktlnewrtHTGIDIAAKEGTPVKAAADGVVVEVGKDPK-YGITVVIDHGNGIKTVYANlD 147

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15600117 182 SRLLVKEGQMVGKGQKIAEAGSS----DADRVQLYFEIRQNG 219
Cdd:COG5821 148 SKIKVKVGQKVKKGQVIGKVGSTalfeSSEGPHLHFEVLKNG 189
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 115-220 5.56e-18

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 79.26  E-value: 5.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117 115 PMKGPVIRRFSSSdklNKGIRIAGTLGQPVQASLAGKVVFAVNNmRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQMVGK 194
Cdd:COG5833 107 PVSGKVVESFQEN---GKGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEA 182

                        90       100
                ....*....|....*....|....*.
gi 15600117 195 GQKIAEAGSSDADRVQLYFEIRQNGR 220
Cdd:COG5833 183 GQKIGTVPATEGEEGTFYFAIKKGGK 208
PRK11637 PRK11637
AmiB activator; Provisional
 114-220 8.17e-17

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 78.58  E-value: 8.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  114 WPMKGPVIRRFSSS--DKLN-KGIRIAGTLGQPVQASLAGKVVFAvNNMRGYGNLVIIQHGTSYTSTYAHNSRLLVKEGQ 190
Cdd:PRK11637 309 WPVRGPTLHRFGEQlqGELRwKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGA 387

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15600117  191 MVGKGQKIAEAGSSDA-DRVQLYFEIRQNGR 220
Cdd:PRK11637 388 QVRAGQPIALVGSSGGqGRPSLYFEIRRQGQ 418
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 36-77 1.59e-13

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: 62.80  E-value: 1.59e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15600117    36 YRVKRGDTLYSIATRHGWNYKDLARANGIRPPYaVKVGQVVR 77
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLK 41
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 36-77 1.02e-12

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: 60.58  E-value: 1.02e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15600117  36 YRVKRGDTLYSIATRHGWNYKDLARANGIRPPYAVKVGQVVR 77
Cdd:cd00118   3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLK 44
LysM smart00257
Lysin motif;
35-77 1.19e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.84  E-value: 1.19e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 15600117     35 EYRVKRGDTLYSIATRHGWNYKDLARANGIRPPYAVKVGQVVR 77
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLK 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
27-77 8.59e-11

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 58.57  E-value: 8.59e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15600117  27 SVPKVVRGEYRVKRGDTLYSIATRHGWNYKDLARANGIRpPYAVKVGQVVR 77
Cdd:COG1388 103 AAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLS-SDTIRPGQKLK 152
PRK11649 PRK11649
putative peptidase; Provisional
 116-204 2.60e-10

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 59.29  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117  116 MKGPVIRRFSSSDKLN--------------KGIRIAGTLGQPVQASLAGKVVFAVNNmRGYGNLVIIQHGTSYTSTYAHN 181
Cdd:PRK11649 284 LRFPTAKQFRISSNFNprrlnpvtgrvaphRGVDFAMPVGTPVLAVGDGEVVVAKRS-GAAGNYVAIRHGRQYTTRYMHL 362

                         90       100
                 ....*....|....*....|...
gi 15600117  182 SRLLVKEGQMVGKGQKIAEAGSS 204
Cdd:PRK11649 363 RKLLVKPGQKVKRGDRIALSGNT 385
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 20-78 7.63e-10

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: 56.17  E-value: 7.63e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600117  20 KAPGPGASVPKVVRGEYRVKRGDTLYSIATRH---GWNYKDLARAN--GIRPPYAVKVGQVVRF 78
Cdd:COG1652  96 EAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 34-99 7.66e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 48.96  E-value: 7.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600117   34 GEYRVKRGDTLYSIATRHGWNYKDLARANGIRPPyAVKVGQVVRFDGRKSTYVASSRSSSNT-RARK 99
Cdd:PRK10783 344 RSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGS-KLKVGQTLTIGAGSSAQRLANNSDSITyRVRK 409
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 36-62 1.51e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 45.11  E-value: 1.51e-05
                         10        20
                 ....*....|....*....|....*..
gi 15600117   36 YRVKRGDTLYSIATRHGWNYKDLARAN 62
Cdd:PRK10783 405 YRVRKGDSLSSIAKRHGVNIKDVMRWN 431
PRK06148 PRK06148
hypothetical protein; Provisional
 141-203 4.44e-04

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 41.16  E-value: 4.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600117   141 GQPVQASLAGKVVFAVNNMR--GYGNLVIIQH----GTSYTSTYAHNSRLLV---KEGQMVGKGQKIAEAGS 203
Cdd:PRK06148  451 GTPVYAPLAGTVRSVEIEAVplGYGGLVALEHetpgGDPFYTLYGHLAHEAVsrlKPGDRLAAGELFGAMGD 522
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 35-79 4.84e-03

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 37.72  E-value: 4.84e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15600117  35 EYRVKRGDTLYSIATRHGWNYKDL---ARANGIRPPYA-VKVGQVVRFD 79
Cdd:COG3061  71 EYTVQSGDTLSQIFRRLGLSASDLyalLAAEGDAKPLSrLKPGQELRFQ 119
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
18-99 6.29e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 37.37  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600117   18 SSKAPGPGASVPKVVrgeYRVKRGDTLYSIATRHGWNYKDLARANGIRPPYaVKVGQVVRFDGRKSTYVASSRSSSNTRA 97
Cdd:PRK06347 393 STSKPSTGTSTNAKV---YTVVKGDSLWRIANNNKVTIANLKSWNNLKSDF-IYPGQKLKVSAGSTSNTNTSKPSTNTNT 468


                 ..
gi 15600117   98 RK 99
Cdd:PRK06347 469 SK 470
 
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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