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Conserved domains on  [gi|57117169|ref|YP_178027|]
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peptidoglycan hydrolase [Mycobacterium tuberculosis H37Rv]

Protein Classification

N-acetylmuramoyl-L-alanine amidase( domain architecture ID 11465562)

N-acetylmuramoyl-L-alanine amidase containing a peptidoglycan binding domain, similar to Mycobacterium tuberculosis peptidoglycan hydrolase CwlM, a cell-wall hydrolase that hydrolyzes the amide bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
181-371 1.67e-52

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


:

Pssm-ID: 440621  Cd Length: 204  Bit Score: 173.91  E-value: 1.67e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 181 VRSSGPKLSGKRIIIDPGRGGVDHGliAQGPAGpISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANA 260
Cdd:COG0860  15 AARKGPPLKGKVIVIDPGHGGKDPG--AIGPNG-LKEKDVNLDIALRLAELLEAPGAKVVLTRDDDTFVSLSERVAIANK 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 261 VGADLMISLRCETQTSLAANGVASFHFGNSHgsVSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDI 340
Cdd:COG0860  92 AKADLFISIHANAAPNPSARGAEVYYYSGSQ--TSAESKKLAEAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVEL 169

                       170       180       190
                ....*....|....*....|....*....|.
gi 57117169 341 GYITNPHDRGMLVSTQTRDAIAEGILAAVKR 371
Cdd:COG0860 170 GFISNPEDEALLKSPAYQQKLAEAIADGILR 200
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 105-161 1.26e-19

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


:

Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 82.26  E-value: 1.26e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57117169 105 GDDVATLQARLQDLGFYTGLVDGHFGLQTHNALMSYQREYGLAADGICGPETLRSLY 161
Cdd:COG3409  12 GEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAALR 68
YcbB super family cl34533
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
8-83 2.95e-15

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


The actual alignment was detected with superfamily member COG2989:

Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 77.29  E-value: 2.95e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57117169   8 DGDALRCGDRSAAVTEIRAALTALGMLDHQEEDLTTgrnvaleLFDAQLDQAVRAFQQHRGLLVDGIVGEATYRAL 83
Cdd:COG2989 200 AGPTLRPGDSDPRVPALRERLAALGDLPADAPSDSD-------VYDAELVEAVKRFQARHGLKADGVIGPATLAAL 268
 
Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
181-371 1.67e-52

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


Pssm-ID: 440621  Cd Length: 204  Bit Score: 173.91  E-value: 1.67e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 181 VRSSGPKLSGKRIIIDPGRGGVDHGliAQGPAGpISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANA 260
Cdd:COG0860  15 AARKGPPLKGKVIVIDPGHGGKDPG--AIGPNG-LKEKDVNLDIALRLAELLEAPGAKVVLTRDDDTFVSLSERVAIANK 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 261 VGADLMISLRCETQTSLAANGVASFHFGNSHgsVSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDI 340
Cdd:COG0860  92 AKADLFISIHANAAPNPSARGAEVYYYSGSQ--TSAESKKLAEAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVEL 169

                       170       180       190
                ....*....|....*....|....*....|.
gi 57117169 341 GYITNPHDRGMLVSTQTRDAIAEGILAAVKR 371
Cdd:COG0860 170 GFISNPEDEALLKSPAYQQKLAEAIADGILR 200
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 192-370 8.24e-47

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.


Pssm-ID: 119407 [Multi-domain]  Cd Length: 172  Bit Score: 158.09  E-value: 8.24e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 192 RIIIDPGRGGVDHGliAQGPAGpISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANAVGADLMISLRC 271
Cdd:cd02696   1 TIVIDPGHGGKDPG--AVGNDG-LKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 272 ETQTSLAANGVASFHFGNShgsvSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDIGYITNPHDRGM 351
Cdd:cd02696  78 NAAPNSSARGAEVYYYSGS----SEESKRLAEAIQKELVKALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKL 153

                       170
                ....*....|....*....
gi 57117169 352 LVSTQTRDAIAEGILAAVK 370
Cdd:cd02696 154 LNSPEYQDKIAEAIAEGIL 172
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 193-371 7.58e-42

N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.


Pssm-ID: 426303  Cd Length: 174  Bit Score: 145.08  E-value: 7.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169   193 IIIDPGRGGVDHGliAQGPAGpISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANAVGADLMISLRCE 272
Cdd:pfam01520   1 IVIDPGHGGKDPG--AVGPNG-ILEKDINLKIALKLRKLLEAKGAEVILTRDSDETVSLEERANIANSNGADLFVSIHAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169   273 TQTSLAANGVASFHFGNshGSVSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDIGYITNPHDRGML 352
Cdd:pfam01520  78 AFPNSSASGVEVYYLAK--RKSSAESKRLAQSIQKELVKVLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLL 155

                         170
                  ....*....|....*....
gi 57117169   353 VSTQTRDAIAEGILAAVKR 371
Cdd:pfam01520 156 NSPAYQQKIAEAIADGILN 174
Ami_3 smart00646
Ami_3 domain;
255-369 2.17e-29

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 110.07  E-value: 2.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169    255 AATANAVGADLMISLRCETQTSLAANGVASFHFGNSHGSvsTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMP 334
Cdd:smart00646   1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGAI--RESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMP 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 57117169    335 TVQVDIGYITNPHDRGMLVSTQTRDAIAEGILAAV 369
Cdd:smart00646  79 AVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 105-161 1.26e-19

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 82.26  E-value: 1.26e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57117169 105 GDDVATLQARLQDLGFYTGLVDGHFGLQTHNALMSYQREYGLAADGICGPETLRSLY 161
Cdd:COG3409  12 GEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAALR 68
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 105-160 9.77e-17

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: 73.70  E-value: 9.77e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 57117169   105 GDDVATLQARLQDLGFYTGLVDGHFGLQTHNALMSYQREYGLAADGICGPETLRSL 160
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
8-83 2.95e-15

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


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 77.29  E-value: 2.95e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57117169   8 DGDALRCGDRSAAVTEIRAALTALGMLDHQEEDLTTgrnvaleLFDAQLDQAVRAFQQHRGLLVDGIVGEATYRAL 83
Cdd:COG2989 200 AGPTLRPGDSDPRVPALRERLAALGDLPADAPSDSD-------VYDAELVEAVKRFQARHGLKADGVIGPATLAAL 268
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 17-83 5.38e-10

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: 54.83  E-value: 5.38e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57117169    17 RSAAVTEIRAALTALGMLDhqeeDLTTGRnvalelFDAQLDQAVRAFQQHRGLLVDGIVGEATYRAL 83
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYP----GPVDGY------FGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
PRK10319 PRK10319
N-acetylmuramoyl-L-alanine amidase AmiA;
169-365 1.33e-09

N-acetylmuramoyl-L-alanine amidase AmiA;


Pssm-ID: 182376 [Multi-domain]  Cd Length: 287  Bit Score: 58.63  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169  169 GGSPHAIREEELVRSSGPKLS-------GKRII-IDPGRGGVDHGLIAQGPAgpiSEADLLWDLASRLEGRMAAIGMETH 240
Cdd:PRK10319  27 SGMSQAIAKEEPLKTSNGHSKpkakksgGKRVVmLDPGHGGIDTGAIGRNGS---KEKHVVLAIAKNVRSILRNHGIDAR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169  241 LSRPTNRSPSDAERAATANAVGADLMISLRCETQTSLAANGVASFHFGNsHGSVSTIGRNLA------------------ 302
Cdd:PRK10319 104 LTRSGDTFIPLYDRVEIAHKHGADLFMSIHADGFTNPKAAGASVFALSN-RGASSAMAKYLSerenradevagkkatdkd 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169  303 --------DFIQREVV------ARTGLRDCR----VHGRTWD-----LLRLTRMPTVQVDIGYITNPHDRGMLVSTQTRD 359
Cdd:PRK10319 183 hllqqvlfDLVQTDTIknsltlGSHILKKIKpvhkLHSRNTEqaafvVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQ 262


                 ....*.
gi 57117169  360 AIAEGI 365
Cdd:PRK10319 263 KIATAI 268
 
Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
181-371 1.67e-52

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


Pssm-ID: 440621  Cd Length: 204  Bit Score: 173.91  E-value: 1.67e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 181 VRSSGPKLSGKRIIIDPGRGGVDHGliAQGPAGpISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANA 260
Cdd:COG0860  15 AARKGPPLKGKVIVIDPGHGGKDPG--AIGPNG-LKEKDVNLDIALRLAELLEAPGAKVVLTRDDDTFVSLSERVAIANK 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 261 VGADLMISLRCETQTSLAANGVASFHFGNSHgsVSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDI 340
Cdd:COG0860  92 AKADLFISIHANAAPNPSARGAEVYYYSGSQ--TSAESKKLAEAIQKELVKALGLKDRGVKQANFYVLRETDMPAVLVEL 169

                       170       180       190
                ....*....|....*....|....*....|.
gi 57117169 341 GYITNPHDRGMLVSTQTRDAIAEGILAAVKR 371
Cdd:COG0860 170 GFISNPEDEALLKSPAYQQKLAEAIADGILR 200
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 192-370 8.24e-47

N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.


Pssm-ID: 119407 [Multi-domain]  Cd Length: 172  Bit Score: 158.09  E-value: 8.24e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 192 RIIIDPGRGGVDHGliAQGPAGpISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANAVGADLMISLRC 271
Cdd:cd02696   1 TIVIDPGHGGKDPG--AVGNDG-LKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169 272 ETQTSLAANGVASFHFGNShgsvSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDIGYITNPHDRGM 351
Cdd:cd02696  78 NAAPNSSARGAEVYYYSGS----SEESKRLAEAIQKELVKALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKL 153

                       170
                ....*....|....*....
gi 57117169 352 LVSTQTRDAIAEGILAAVK 370
Cdd:cd02696 154 LNSPEYQDKIAEAIAEGIL 172
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 193-371 7.58e-42

N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.


Pssm-ID: 426303  Cd Length: 174  Bit Score: 145.08  E-value: 7.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169   193 IIIDPGRGGVDHGliAQGPAGpISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANAVGADLMISLRCE 272
Cdd:pfam01520   1 IVIDPGHGGKDPG--AVGPNG-ILEKDINLKIALKLRKLLEAKGAEVILTRDSDETVSLEERANIANSNGADLFVSIHAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169   273 TQTSLAANGVASFHFGNshGSVSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDIGYITNPHDRGML 352
Cdd:pfam01520  78 AFPNSSASGVEVYYLAK--RKSSAESKRLAQSIQKELVKVLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLL 155

                         170
                  ....*....|....*....
gi 57117169   353 VSTQTRDAIAEGILAAVKR 371
Cdd:pfam01520 156 NSPAYQQKIAEAIADGILN 174
Ami_3 smart00646
Ami_3 domain;
255-369 2.17e-29

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 110.07  E-value: 2.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169    255 AATANAVGADLMISLRCETQTSLAANGVASFHFGNSHGSvsTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMP 334
Cdd:smart00646   1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGAI--RESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMP 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 57117169    335 TVQVDIGYITNPHDRGMLVSTQTRDAIAEGILAAV 369
Cdd:smart00646  79 AVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 105-161 1.26e-19

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 82.26  E-value: 1.26e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57117169 105 GDDVATLQARLQDLGFYTGLVDGHFGLQTHNALMSYQREYGLAADGICGPETLRSLY 161
Cdd:COG3409  12 GEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAALR 68
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 105-160 9.77e-17

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: 73.70  E-value: 9.77e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 57117169   105 GDDVATLQARLQDLGFYTGLVDGHFGLQTHNALMSYQREYGLAADGICGPETLRSL 160
Cdd:pfam01471   2 GEDVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
8-83 2.95e-15

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


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 77.29  E-value: 2.95e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57117169   8 DGDALRCGDRSAAVTEIRAALTALGMLDHQEEDLTTgrnvaleLFDAQLDQAVRAFQQHRGLLVDGIVGEATYRAL 83
Cdd:COG2989 200 AGPTLRPGDSDPRVPALRERLAALGDLPADAPSDSD-------VYDAELVEAVKRFQARHGLKADGVIGPATLAAL 268
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 11-85 1.90e-11

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 59.15  E-value: 1.90e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57117169  11 ALRCGDRSAAVTEIRAALTALGmLDHQEEDlttGRnvalelFDAQLDQAVRAFQQHRGLLVDGIVGEATYRALKE 85
Cdd:COG3409   5 TLRLGDSGEDVRELQQRLNALG-YYPGPVD---GI------FGPATEAAVRAFQRANGLPVDGIVGPATWAALRA 69
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 17-83 5.38e-10

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: 54.83  E-value: 5.38e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57117169    17 RSAAVTEIRAALTALGMLDhqeeDLTTGRnvalelFDAQLDQAVRAFQQHRGLLVDGIVGEATYRAL 83
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYP----GPVDGY------FGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
PRK10319 PRK10319
N-acetylmuramoyl-L-alanine amidase AmiA;
169-365 1.33e-09

N-acetylmuramoyl-L-alanine amidase AmiA;


Pssm-ID: 182376 [Multi-domain]  Cd Length: 287  Bit Score: 58.63  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169  169 GGSPHAIREEELVRSSGPKLS-------GKRII-IDPGRGGVDHGLIAQGPAgpiSEADLLWDLASRLEGRMAAIGMETH 240
Cdd:PRK10319  27 SGMSQAIAKEEPLKTSNGHSKpkakksgGKRVVmLDPGHGGIDTGAIGRNGS---KEKHVVLAIAKNVRSILRNHGIDAR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169  241 LSRPTNRSPSDAERAATANAVGADLMISLRCETQTSLAANGVASFHFGNsHGSVSTIGRNLA------------------ 302
Cdd:PRK10319 104 LTRSGDTFIPLYDRVEIAHKHGADLFMSIHADGFTNPKAAGASVFALSN-RGASSAMAKYLSerenradevagkkatdkd 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57117169  303 --------DFIQREVV------ARTGLRDCR----VHGRTWD-----LLRLTRMPTVQVDIGYITNPHDRGMLVSTQTRD 359
Cdd:PRK10319 183 hllqqvlfDLVQTDTIknsltlGSHILKKIKpvhkLHSRNTEqaafvVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQ 262


                 ....*.
gi 57117169  360 AIAEGI 365
Cdd:PRK10319 263 KIATAI 268
 
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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