NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|513881722|ref|WP_016527138|]
View 

LysM peptidoglycan-binding domain-containing protein [Lactiplantibacillus plantarum]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
23-143 2.18e-15

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 75.50  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513881722  23 ATGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKAsdgniDLIYVGQNLQIGGSATKTATTKSATKKA----AT 98
Cdd:PRK06347 472 STNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKS-----DFIYPGQKLKVSAGSTTNNTNTAKPSTNkpsnST 546
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 513881722  99 KGTYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK06347 547 VKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
23-143 2.18e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 75.50  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513881722  23 ATGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKAsdgniDLIYVGQNLQIGGSATKTATTKSATKKA----AT 98
Cdd:PRK06347 472 STNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKS-----DFIYPGQKLKVSAGSTTNNTNTAKPSTNkpsnST 546
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 513881722  99 KGTYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK06347 547 VKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
101-146 2.89e-14

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.58  E-value: 2.89e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 513881722 101 TYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQVPGA 146
Cdd:COG1388  111 TYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
102-144 1.92e-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: 63.18  E-value: 1.92e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 513881722  102 YTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQVP 144
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
101-143 1.94e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 57.50  E-value: 1.94e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 513881722 101 TYTVKAGDTLWALADKYNTSVHALQTLNGL-SGDLIVVGQNIQV 143
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
101-143 5.05e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.69  E-value: 5.05e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 513881722   101 TYTVKAGDTLWALADKYNTSVHALQTLNG-LSGDLIVVGQNIQV 143
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
23-143 2.18e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 75.50  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513881722  23 ATGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKAsdgniDLIYVGQNLQIGGSATKTATTKSATKKA----AT 98
Cdd:PRK06347 472 STNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKS-----DFIYPGQKLKVSAGSTTNNTNTAKPSTNkpsnST 546
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 513881722  99 KGTYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK06347 547 VKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
23-143 1.17e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 73.58  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513881722  23 ATGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKAsdgniDLIYVGQNLQIGGSATKTA----------TTKSA 92
Cdd:PRK06347 398 STGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKS-----DFIYPGQKLKVSAGSTSNTntskpstntnTSKPS 472
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 513881722  93 TKKAATKGTYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK06347 473 TNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV 523
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
24-143 1.72e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 73.19  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513881722  24 TGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKAsdgniDLIYVGQNLQIGGSATKTATTKS-----------A 92
Cdd:PRK06347 324 TGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKS-----DFIYPGQKLKVSAGSTTSDTNTSkpstgtstskpS 398
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 513881722  93 TKKAATKGTYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK06347 399 TGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV 449
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
101-146 2.89e-14

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.58  E-value: 2.89e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 513881722 101 TYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQVPGA 146
Cdd:COG1388  111 TYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
102-144 1.92e-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: 63.18  E-value: 1.92e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 513881722  102 YTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQVP 144
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
101-143 1.94e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 57.50  E-value: 1.94e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 513881722 101 TYTVKAGDTLWALADKYNTSVHALQTLNGL-SGDLIVVGQNIQV 143
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
101-143 5.05e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 56.69  E-value: 5.05e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 513881722   101 TYTVKAGDTLWALADKYNTSVHALQTLNG-LSGDLIVVGQNIQV 143
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
34-79 3.41e-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: 51.33  E-value: 3.41e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 513881722  34 TVKANDTVWGLAQQHGVSVQSIEKLNQIKasdgNIDLIYVGQNLQI 79
Cdd:cd00118    4 TVKPGDTLWSIAKKYGVTVEELAAANPLI----NPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
24-79 9.33e-09

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 53.56  E-value: 9.33e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 513881722  24 TGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKAsdgniDLIYVGQNLQI 79
Cdd:COG1388  103 AAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-----DTIRPGQKLKI 153
LysM smart00257
Lysin motif;
33-79 9.70e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 50.14  E-value: 9.70e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 513881722    33 ITVKANDTVWGLAQQHGVSVQSIEKLNQIKASdgniDLIYVGQNLQI 79
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDP----DNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
33-79 2.02e-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: 49.32  E-value: 2.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 513881722   33 ITVKANDTVWGLAQQHGVSVQSIEKLNQIKASDgnidlIYVGQNLQI 79
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-----LYVGQKLKI 42
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
100-143 8.36e-08

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 52.81  E-value: 8.36e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 513881722 100 GTYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK10783 344 RSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
PRK13914 PRK13914
invasion associated endopeptidase;
101-143 3.22e-07

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 50.96  E-value: 3.22e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 513881722 101 TYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK13914 201 THAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAI 243
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
20-145 3.52e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 50.89  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513881722  20 LLLATGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKASdgnidLIYVGQNLQIGGSATKTATTKSATKKaatk 99
Cdd:PRK10783 333 TLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGS-----KLKVGQTLTIGAGSSAQRLANNSDSI---- 403
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 513881722 100 gTYTVKAGDTLWALADKYNTSVHALQTLNGlsgdliVVGQNIQvPG 145
Cdd:PRK10783 404 -TYRVRKGDSLSSIAKRHGVNIKDVMRWNS------DTAKNLQ-PG 441
PRK13914 PRK13914
invasion associated endopeptidase;
11-79 2.45e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 48.26  E-value: 2.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 513881722  11 LASTVGAVGLLLATGQAANAASITVKANDTVWGLAQQHGVSVQSIEKLNQIKAsdgniDLIYVGQNLQI 79
Cdd:PRK13914   8 IAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTT-----DKIVPGQKLQV 71
PRK13914 PRK13914
invasion associated endopeptidase;
101-143 7.70e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 46.72  E-value: 7.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 513881722 101 TYTVKAGDTLWALADKYNTSVHALQTLNGLSGDLIVVGQNIQV 143
Cdd:PRK13914  29 TVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
1-79 4.23e-04

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: 39.99  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513881722   1 MSQAHTTGKVLASTVGAVGLLLATGQAANAASI-TVKANDTVWGLAQQH---GVSVQSIEKLN--QIKasdgNIDLIYVG 74
Cdd:COG1652   79 MRAGAAAKLSPAVTVAEEAAAPSAELAPDAPKTyTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIK----NPDLIYPG 154

                 ....*
gi 513881722  75 QNLQI 79
Cdd:COG1652  155 QVLRI 159
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
101-144 1.54e-03

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: 38.45  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 513881722 101 TYTVKAGDTLWALADKY---NTSVHALQTLNGL---SGDLIVVGQNIQVP 144
Cdd:COG1652  111 TYTVKPGDTLWGIAKRFygdPARWPEIAEANRDqikNPDLIYPGQVLRIP 160
PRK14125 PRK14125
cell division suppressor protein YneA; Provisional
101-144 2.84e-03

cell division suppressor protein YneA; Provisional


Pssm-ID: 184523 [Multi-domain]  Cd Length: 103  Bit Score: 36.55  E-value: 2.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 513881722 101 TYTVKAGDTLWALADKYNTSVHALQT--------LNGLSGDLIVVGQNIQVP 144
Cdd:PRK14125  38 EITVQEGDTLWALADQYAGKHHMAKNefiewvedVNNLPSGHIKAGDKLVIP 89
 
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