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Conserved domains on  [gi|1934801810|ref|WP_195727878|]
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MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-164 1.44e-74

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 444359  Cd Length: 177  Bit Score: 226.00  E-value: 1.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810   1 MINIIQDFIPVGANNRPGYAMTPLYITVHNTANTAVGADAAAhaRYLKNPGTTTSWHFTVDDTEIYQHLPLNENGWHAGD 80
Cdd:COG5632     2 GVNIKKKLIPKNNSYRPGYKMKPKGIVIHNTANPGATAENHA--NYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  81 GNGSGNRASIGIEICENADGDFAKATANAQWLIKTLMAEHNISVANVVPHKYWSGKECPRKLLD----TWDSFKAGIGGG 156
Cdd:COG5632    80 GTGPGNRRSIGIEICENKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLAnggyRWDQFKADVKSA 159


                  ....*...
gi 1934801810 157 GSQTYVVK 164
Cdd:COG5632   160 LNGLSTVK 167
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 159-203 8.04e-18

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: 75.21  E-value: 8.04e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1934801810 159 QTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLIRVGQVLIV 203
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 230-292 2.97e-17

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 74.56  E-value: 2.97e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934801810 230 SGEHVFQVQRALAALYFYPDKgavnngIDGVYGPKTADAVARFQSVNGLTADGIYGPPTKAKI 292
Cdd:COG3409    11 SGEDVRELQQRLNALGYYPGP------VDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAAL 67
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-164 1.44e-74

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 226.00  E-value: 1.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810   1 MINIIQDFIPVGANNRPGYAMTPLYITVHNTANTAVGADAAAhaRYLKNPGTTTSWHFTVDDTEIYQHLPLNENGWHAGD 80
Cdd:COG5632     2 GVNIKKKLIPKNNSYRPGYKMKPKGIVIHNTANPGATAENHA--NYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  81 GNGSGNRASIGIEICENADGDFAKATANAQWLIKTLMAEHNISVANVVPHKYWSGKECPRKLLD----TWDSFKAGIGGG 156
Cdd:COG5632    80 GTGPGNRRSIGIEICENKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLAnggyRWDQFKADVKSA 159


                  ....*...
gi 1934801810 157 GSQTYVVK 164
Cdd:COG5632   160 LNGLSTVK 167
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 22-141 4.90e-28

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 104.75  E-value: 4.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  22 TPLYITVHNTANTAVGADAAAHARYLKNPGTTTSWHFTVD-DTEIYQHLPLNENGWHAGDGNgsGNRASIGIEICENADG 100
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAACIARGWSDVSYHYLIDrDGTIYQLVPENGRAWHAGNGG--GNDRSIGIELEGNFGG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934801810 101 D--FAKATANAQWLIKTLMAEHNISV-ANVVPHKYWSGKECPRK 141
Cdd:pfam01510  79 DppTDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 23-140 6.40e-28

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 104.68  E-value: 6.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  23 PLYITVHNTANTAVGADAAAHaRYLKNP----GTTTSWHFTVD-DTEIYQHLPLNENGWHAGdgnGSGNRASIGIEICEN 97
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAAAV-RYLQNYhmrgWSDISYHFLVGgDGRIYQGRGWNYVGWHAG---GNYNSYSIGIELIGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1934801810  98 ADGD--FAKATANAQWLIKTLMAEHNISVA-NVVPHKYWSG-KECPR 140
Cdd:cd06583    78 FDGGppTAAQLEALAELLAYLVKRYGIPPDyRIVGHRDVSPgTECPG 124
Ami_2 smart00644
Ami_2 domain;
21-139 1.24e-27

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 103.98  E-value: 1.24e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810   21 MTPLYITVHNTANTAVGADAAAhaRYLKNPGTT-TSWHFTVD-DTEIYQHLPLNENGWHAGDGN-GSGNRASIGIEICEN 97
Cdd:smart00644   1 PPPRGIVIHHTANSNASCANEA--RYMQNNHMNdIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHtPGYNDISIGIEFIGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1934801810   98 ADGD---FAKATANAQWLIKTLMAEHNISVA---NVVPHKYWSGKECP 139
Cdd:smart00644  79 FDSDdepFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 159-203 8.04e-18

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: 75.21  E-value: 8.04e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1934801810 159 QTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLIRVGQVLIV 203
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
156-206 1.68e-17

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 77.83  E-value: 1.68e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934801810 156 GGSQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDpNLIRVGQVLIVSAP 206
Cdd:COG1388   107 PSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKIPAS 156
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 230-292 2.97e-17

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 74.56  E-value: 2.97e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934801810 230 SGEHVFQVQRALAALYFYPDKgavnngIDGVYGPKTADAVARFQSVNGLTADGIYGPPTKAKI 292
Cdd:COG3409    11 SGEDVRELQQRLNALGYYPGP------VDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAAL 67
LysM smart00257
Lysin motif;
160-203 1.69e-16

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 71.71  E-value: 1.69e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1934801810  160 TYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLIRVGQVLIV 203
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 230-292 7.27e-16

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 70.24  E-value: 7.27e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934801810 230 SGEHVFQVQRALAALYFYPDKgavnngIDGVYGPKTADAVARFQSVNGLTADGIYGPPTKAKI 292
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP------VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 161-203 1.38e-15

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: 69.35  E-value: 1.38e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1934801810 161 YVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNlIRVGQVLIV 203
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 158-211 1.95e-09

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 57.82  E-value: 1.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1934801810 158 SQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLiRVGQVLIVSAPSSTEE 211
Cdd:PRK10783  343 SRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKL-KVGQTLTIGAGSSAQR 395
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
100-294 4.77e-08

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 53.93  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810 100 GDFAKATANAQWLiKTLMAEHNISvanvvphKYWSGKECPRKLLDTWDSFKAGIGGGGS--QTYVVKQGDTLTSIARAFG 177
Cdd:PRK06347  278 GTYATDTAYATKL-NDLISRYNLT-------QYDSGKTTGGNSGSTGNSSNSSNTGNTSnaKIYTVVKGDSLWRIANNHK 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810 178 VTVAQLQEWNNIEDPNlIRVGQVLIVSAPSSTEEPEPYPlPDGIIQLATPYTSGE---HVFQVQRAlAALYfypdKGAVN 254
Cdd:PRK06347  350 VTVANLKAWNNLKSDF-IYPGQKLKVSAGSTTSDTNTSK-PSTGTSTSKPSTGTStnaKVYTVVKG-DSLW----RIANN 422

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1934801810 255 NGIdgvygpktadAVARFQSVNGLTADGIYgPPTKAKIAA 294
Cdd:PRK06347  423 NKV----------TIANLKSWNNLKSDFIY-PGQKLKVSA 451
PRK10594 PRK10594
murein L,D-transpeptidase; Provisional
 258-289 4.10e-03

murein L,D-transpeptidase; Provisional


Pssm-ID: 236723 [Multi-domain]  Cd Length: 608  Bit Score: 38.57  E-value: 4.10e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1934801810 258 DGVYGPKTADAVARFQSVNGLTADGIYGPPTK 289
Cdd:PRK10594  306 RAAYDNELVEAVKRFQAWQGLGADGVIGPRTR 337
 
Name Accession Description Interval E-value
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
1-164 1.44e-74

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 226.00  E-value: 1.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810   1 MINIIQDFIPVGANNRPGYAMTPLYITVHNTANTAVGADAAAhaRYLKNPGTTTSWHFTVDDTEIYQHLPLNENGWHAGD 80
Cdd:COG5632     2 GVNIKKKLIPKNNSYRPGYKMKPKGIVIHNTANPGATAENHA--NYFNNNNRSASWHYFVDDKEIIQHIPLNENAWHAGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  81 GNGSGNRASIGIEICENADGDFAKATANAQWLIKTLMAEHNISVANVVPHKYWSGKECPRKLLD----TWDSFKAGIGGG 156
Cdd:COG5632    80 GTGPGNRRSIGIEICENKDGDFAKAYENAAELIAYLMKKYGIPIDNVVRHYDWSGKNCPHGLLAnggyRWDQFKADVKSA 159


                  ....*...
gi 1934801810 157 GSQTYVVK 164
Cdd:COG5632   160 LNGLSTVK 167
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 22-141 4.90e-28

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 104.75  E-value: 4.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  22 TPLYITVHNTANTAVGADAAAHARYLKNPGTTTSWHFTVD-DTEIYQHLPLNENGWHAGDGNgsGNRASIGIEICENADG 100
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAACIARGWSDVSYHYLIDrDGTIYQLVPENGRAWHAGNGG--GNDRSIGIELEGNFGG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934801810 101 D--FAKATANAQWLIKTLMAEHNISV-ANVVPHKYWSGKECPRK 141
Cdd:pfam01510  79 DppTDAQYEALARLLADLCKRYGIPPdRRIVGHRDVGRKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 23-140 6.40e-28

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 104.68  E-value: 6.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  23 PLYITVHNTANTAVGADAAAHaRYLKNP----GTTTSWHFTVD-DTEIYQHLPLNENGWHAGdgnGSGNRASIGIEICEN 97
Cdd:cd06583     2 VKYVVIHHTANPNCYTAAAAV-RYLQNYhmrgWSDISYHFLVGgDGRIYQGRGWNYVGWHAG---GNYNSYSIGIELIGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1934801810  98 ADGD--FAKATANAQWLIKTLMAEHNISVA-NVVPHKYWSG-KECPR 140
Cdd:cd06583    78 FDGGppTAAQLEALAELLAYLVKRYGIPPDyRIVGHRDVSPgTECPG 124
Ami_2 smart00644
Ami_2 domain;
21-139 1.24e-27

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 103.98  E-value: 1.24e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810   21 MTPLYITVHNTANTAVGADAAAhaRYLKNPGTT-TSWHFTVD-DTEIYQHLPLNENGWHAGDGN-GSGNRASIGIEICEN 97
Cdd:smart00644   1 PPPRGIVIHHTANSNASCANEA--RYMQNNHMNdIGYHFLVGgDGRVYQGVGWNYVAWHAGGAHtPGYNDISIGIEFIGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1934801810   98 ADGD---FAKATANAQWLIKTLMAEHNISVA---NVVPHKYWSGKECP 139
Cdd:smart00644  79 FDSDdepFAEALYAALDLLAKLLKGAGLPPDgryRIVGHRDVAPTEDP 126
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
14-157 1.05e-20

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 86.84  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810  14 NNRPGyAMTPLYITVHNTANTAVGADAaahaRYLKNPGTTTSWHFTVD-DTEIYQHLPLNENGWHAGDGNGSG----NRA 88
Cdd:COG3023    19 DERPA-GAEIDLIVIHYTAGPPGGGAL----DWLTDPALRVSAHYLIDrDGEIYQLVPEDDRAWHAGVSSWRGrtnlNDF 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934801810  89 SIGIEIcENADGDFAKATAnAQ-----WLIKTLMAEHNISVANVVPHKYWSG--KECPRKLLDtWDSFKAGIGGGG 157
Cdd:COG3023    94 SIGIEL-ENPGHGWAPFTE-AQyealaALLRDLCARYGIPPDHIVGHSDIAPgrKTDPGPAFP-WARLAALLARYG 166
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 159-203 8.04e-18

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: 75.21  E-value: 8.04e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1934801810 159 QTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLIRVGQVLIV 203
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
156-206 1.68e-17

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 77.83  E-value: 1.68e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934801810 156 GGSQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDpNLIRVGQVLIVSAP 206
Cdd:COG1388   107 PSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKIPAS 156
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 230-292 2.97e-17

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 74.56  E-value: 2.97e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934801810 230 SGEHVFQVQRALAALYFYPDKgavnngIDGVYGPKTADAVARFQSVNGLTADGIYGPPTKAKI 292
Cdd:COG3409    11 SGEDVRELQQRLNALGYYPGP------VDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAAL 67
LysM smart00257
Lysin motif;
160-203 1.69e-16

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 71.71  E-value: 1.69e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1934801810  160 TYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLIRVGQVLIV 203
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 230-292 7.27e-16

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 70.24  E-value: 7.27e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934801810 230 SGEHVFQVQRALAALYFYPDKgavnngIDGVYGPKTADAVARFQSVNGLTADGIYGPPTKAKI 292
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP------VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 161-203 1.38e-15

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: 69.35  E-value: 1.38e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1934801810 161 YVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNlIRVGQVLIV 203
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 158-211 1.95e-09

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 57.82  E-value: 1.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1934801810 158 SQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLiRVGQVLIVSAPSSTEE 211
Cdd:PRK10783  343 SRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKL-KVGQTLTIGAGSSAQR 395
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 151-203 5.17e-09

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: 54.63  E-value: 5.17e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1934801810 151 AGIGGGGSQTYVVKQGDTLTSIARAFGVTVAQLQEW-----NNIEDPNLIRVGQVLIV 203
Cdd:COG1652   102 AELAPDAPKTYTVKPGDTLWGIAKRFYGDPARWPEIaeanrDQIKNPDLIYPGQVLRI 159
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
100-294 4.77e-08

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 53.93  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810 100 GDFAKATANAQWLiKTLMAEHNISvanvvphKYWSGKECPRKLLDTWDSFKAGIGGGGS--QTYVVKQGDTLTSIARAFG 177
Cdd:PRK06347  278 GTYATDTAYATKL-NDLISRYNLT-------QYDSGKTTGGNSGSTGNSSNSSNTGNTSnaKIYTVVKGDSLWRIANNHK 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810 178 VTVAQLQEWNNIEDPNlIRVGQVLIVSAPSSTEEPEPYPlPDGIIQLATPYTSGE---HVFQVQRAlAALYfypdKGAVN 254
Cdd:PRK06347  350 VTVANLKAWNNLKSDF-IYPGQKLKVSAGSTTSDTNTSK-PSTGTSTSKPSTGTStnaKVYTVVKG-DSLW----RIANN 422

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1934801810 255 NGIdgvygpktadAVARFQSVNGLTADGIYgPPTKAKIAA 294
Cdd:PRK06347  423 NKV----------TIANLKSWNNLKSDFIY-PGQKLKVSA 451
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
158-294 1.30e-07

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 52.77  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934801810 158 SQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDpNLIRVGQVLIVSAPSSTEEPEPYPLPDGIIQLATPYTS-GEHVFQ 236
Cdd:PRK06347  405 AKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKS-DFIYPGQKLKVSAGSTSNTNTSKPSTNTNTSKPSTNTNtNAKVYT 483

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1934801810 237 VQRAlAALYfypdKGAVNNGIdgvygpktadAVARFQSVNGLTADGIYgPPTKAKIAA 294
Cdd:PRK06347  484 VAKG-DSLW----RIANNNKV----------TIANLKSWNNLKSDFIY-PGQKLKVSA 525
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
158-209 6.24e-07

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 50.46  E-value: 6.24e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1934801810 158 SQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNlIRVGQVLIVSAPSST 209
Cdd:PRK06347  479 AKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDF-IYPGQKLKVSAGSTT 529
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
159-203 4.95e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 44.69  E-value: 4.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1934801810 159 QTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDpNLIRVGQVLIV 203
Cdd:PRK06347  548 KTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTS-NMIHVGQKLTI 591
PRK13914 PRK13914
invasion associated endopeptidase;
160-213 5.04e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 44.41  E-value: 5.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1934801810 160 TYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNlIRVGQVLIVSAPSSTEEPE 213
Cdd:PRK13914  201 THAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAIKQTANTATPK 253
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
210-288 5.24e-05

Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 44.55  E-value: 5.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934801810 210 EEPEPYPLPDGiiQLATPYTSGEHVFQVQRALAALYFYPDKGAVNngiDGVYGPKTADAVARFQSVNGLTADGIYGPPT 288
Cdd:COG2989   191 AAGGWPPVPAG--PTLRPGDSDPRVPALRERLAALGDLPADAPSD---SDVYDAELVEAVKRFQARHGLKADGVIGPAT 264
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 153-194 5.95e-05

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.34  E-value: 5.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1934801810 153 IGGGGSQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNL 194
Cdd:PRK10783  397 ANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNL 438
nlpD PRK10871
murein hydrolase activator NlpD;
154-209 7.92e-04

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 40.59  E-value: 7.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1934801810 154 GGGGSQTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNLIRVGQVLIVSAPSST 209
Cdd:PRK10871   56 GSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASGT 111
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 159-201 3.99e-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: 38.49  E-value: 3.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1934801810 159 QTYVVKQGDTLTSIARAFGVTVAQLQEWNNIEDPNL----IRVGQVL 201
Cdd:COG3061    70 QEYTVQSGDTLSQIFRRLGLSASDLYALLAAEGDAKplsrLKPGQEL 116
PRK10594 PRK10594
murein L,D-transpeptidase; Provisional
 258-289 4.10e-03

murein L,D-transpeptidase; Provisional


Pssm-ID: 236723 [Multi-domain]  Cd Length: 608  Bit Score: 38.57  E-value: 4.10e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1934801810 258 DGVYGPKTADAVARFQSVNGLTADGIYGPPTK 289
Cdd:PRK10594  306 RAAYDNELVEAVKRFQAWQGLGADGVIGPRTR 337
 
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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