NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1519253197|gb|AZA12427|]
View 

N-acetylmuramoyl-L-alanine amidase AmiA precursor [Corynebacterium gerontici]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
172-373 2.05e-46

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


:

Pssm-ID: 440621  Cd Length: 204  Bit Score: 157.74  E-value: 2.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 172 LRERERVRDAGPRLAGKRVVIDPSLGGNNRGQVVKGRfgeISEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSR 251
Cdd:COG0860     9 LAAAPAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNG---LKEKDVNLDIALRLAELLEAPGAKVVLTRDDDTFVSLSER 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 252 AEIANAFGADLMLCLQADKYQNEKASGCASFYFGSEVGSSSliGELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMP 331
Cdd:COG0860    86 VAIANKAKADLFISIHANAAPNPSARGAEVYYYSGSQTSAE--SKKLAEAIQKELVKALGLKDRGVKQANFYVLRETDMP 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1519253197 332 TVEVVVGYLTNPEDVKILTDPASRDAIAEAIVVAVKRlYLQE 373
Cdd:COG0860   164 AVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILR-YFGK 204
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 114-156 8.90e-12

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


:

Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 59.92  E-value: 8.90e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1519253197 114 ELGFYTDRLDGRFGEETHAALMNYQMNYGLQADGICGPETIRA 156
Cdd:COG3409    24 ALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAA 66
YcbB super family cl34533
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
5-80 1.83e-11

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: 65.35  E-value: 1.83e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519253197   5 LRVGDRSARVAEVRDALARLGFLQGTDKQVSNakgrtfteaekLFDEPLADALKAFQQTRGIIASGVINDPTLRVL 80
Cdd:COG2989   204 LRPGDSDPRVPALRERLAALGDLPADAPSDSD-----------VYDAELVEAVKRFQARHGLKADGVIGPATLAAL 268
 
Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
172-373 2.05e-46

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


Pssm-ID: 440621  Cd Length: 204  Bit Score: 157.74  E-value: 2.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 172 LRERERVRDAGPRLAGKRVVIDPSLGGNNRGQVVKGRfgeISEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSR 251
Cdd:COG0860     9 LAAAPAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNG---LKEKDVNLDIALRLAELLEAPGAKVVLTRDDDTFVSLSER 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 252 AEIANAFGADLMLCLQADKYQNEKASGCASFYFGSEVGSSSliGELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMP 331
Cdd:COG0860    86 VAIANKAKADLFISIHANAAPNPSARGAEVYYYSGSQTSAE--SKKLAEAIQKELVKALGLKDRGVKQANFYVLRETDMP 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1519253197 332 TVEVVVGYLTNPEDVKILTDPASRDAIAEAIVVAVKRlYLQE 373
Cdd:COG0860   164 AVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILR-YFGK 204
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 190-368 1.32e-40

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: 141.61  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 190 VVIDPSLGGNNRGQVvkGRFGeISEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSRAEIANAFGADLMLCLQAD 269
Cdd:pfam01520   1 IVIDPGHGGKDPGAV--GPNG-ILEKDINLKIALKLRKLLEAKGAEVILTRDSDETVSLEERANIANSNGADLFVSIHAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 270 KYQNEKASGCASFYfgSEVGSSSLIGELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMPTVEVVVGYLTNPEDVKIL 349
Cdd:pfam01520  78 AFPNSSASGVEVYY--LAKRKSSAESKRLAQSIQKELVKVLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLL 155

                         170
                  ....*....|....*....
gi 1519253197 350 TDPASRDAIAEAIVVAVKR 368
Cdd:pfam01520 156 NSPAYQQKIAEAIADGILN 174
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 189-367 5.61e-40

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: 139.98  E-value: 5.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 189 RVVIDPSLGGNNRGQVvkGRFGeISEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSRAEIANAFGADLMLCLQA 268
Cdd:cd02696     1 TIVIDPGHGGKDPGAV--GNDG-LKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 269 DKYQNEKASGCASFYFGSEVGSSsligELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMPTVEVVVGYLTNPEDVKI 348
Cdd:cd02696    78 NAAPNSSARGAEVYYYSGSSEES----KRLAEAIQKELVKALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKL 153

                         170
                  ....*....|....*....
gi 1519253197 349 LTDPASRDAIAEAIVVAVK 367
Cdd:cd02696   154 LNSPEYQDKIAEAIAEGIL 172
Ami_3 smart00646
Ami_3 domain;
252-366 4.99e-22

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 90.04  E-value: 4.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197  252 AEIANAFGADLMLCLQADKYQNEKASGCASFYFGSevGSSSLIGELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMP 331
Cdd:smart00646   1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSD--KGAIRESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMP 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1519253197  332 TVEVVVGYLTNPEDVKILTDPASRDAIAEAIVVAV 366
Cdd:smart00646  79 AVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
PRK10319 PRK10319
N-acetylmuramoyl-L-alanine amidase AmiA;
183-377 3.62e-12

N-acetylmuramoyl-L-alanine amidase AmiA;


Pssm-ID: 182376 [Multi-domain]  Cd Length: 287  Bit Score: 66.34  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 183 PRLAGKR-VVIDPSLGGNNRGQVvkGRFGEiSEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSRAEIANAFGAD 261
Cdd:PRK10319   51 KKSGGKRvVMLDPGHGGIDTGAI--GRNGS-KEKHVVLAIAKNVRSILRNHGIDARLTRSGDTFIPLYDRVEIAHKHGAD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 262 LMLCLQADKYQNEKASGcASFYFGSEVGSSSLIGELLSgfiQREIVA-----------------------RTNLIN---- 314
Cdd:PRK10319  128 LFMSIHADGFTNPKAAG-ASVFALSNRGASSAMAKYLS---ERENRAdevagkkatdkdhllqqvlfdlvQTDTIKnslt 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 315 CGNH-----------------GRTWDLLRVTQMPTVEVVVGYLTNPEDVKILTDPASRDAIAEAIVVAVKRlYLQEQDDQ 377
Cdd:PRK10319  204 LGSHilkkikpvhklhsrnteQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQKIATAIAEGIIS-YFHWFDNQ 282
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 114-156 8.90e-12

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 59.92  E-value: 8.90e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1519253197 114 ELGFYTDRLDGRFGEETHAALMNYQMNYGLQADGICGPETIRA 156
Cdd:COG3409    24 ALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAA 66
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
5-80 1.83e-11

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


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 65.35  E-value: 1.83e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519253197   5 LRVGDRSARVAEVRDALARLGFLQGTDKQVSNakgrtfteaekLFDEPLADALKAFQQTRGIIASGVINDPTLRVL 80
Cdd:COG2989   204 LRPGDSDPRVPALRERLAALGDLPADAPSDSD-----------VYDAELVEAVKRFQARHGLKADGVIGPATLAAL 268
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 115-156 1.28e-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: 56.37  E-value: 1.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1519253197 115 LGFYTDRLDGRFGEETHAALMNYQMNYGLQADGICGPETIRA 156
Cdd:pfam01471  15 LGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAA 56
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 10-80 2.59e-05

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: 41.35  E-value: 2.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519253197  10 RSARVAEVRDALARLGFLQGTdkqvsnakgrtfteAEKLFDEPLADALKAFQQTRGIIASGVINDPTLRVL 80
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP--------------VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
172-373 2.05e-46

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


Pssm-ID: 440621  Cd Length: 204  Bit Score: 157.74  E-value: 2.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 172 LRERERVRDAGPRLAGKRVVIDPSLGGNNRGQVVKGRfgeISEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSR 251
Cdd:COG0860     9 LAAAPAAARKGPPLKGKVIVIDPGHGGKDPGAIGPNG---LKEKDVNLDIALRLAELLEAPGAKVVLTRDDDTFVSLSER 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 252 AEIANAFGADLMLCLQADKYQNEKASGCASFYFGSEVGSSSliGELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMP 331
Cdd:COG0860    86 VAIANKAKADLFISIHANAAPNPSARGAEVYYYSGSQTSAE--SKKLAEAIQKELVKALGLKDRGVKQANFYVLRETDMP 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1519253197 332 TVEVVVGYLTNPEDVKILTDPASRDAIAEAIVVAVKRlYLQE 373
Cdd:COG0860   164 AVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILR-YFGK 204
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 190-368 1.32e-40

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: 141.61  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 190 VVIDPSLGGNNRGQVvkGRFGeISEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSRAEIANAFGADLMLCLQAD 269
Cdd:pfam01520   1 IVIDPGHGGKDPGAV--GPNG-ILEKDINLKIALKLRKLLEAKGAEVILTRDSDETVSLEERANIANSNGADLFVSIHAN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 270 KYQNEKASGCASFYfgSEVGSSSLIGELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMPTVEVVVGYLTNPEDVKIL 349
Cdd:pfam01520  78 AFPNSSASGVEVYY--LAKRKSSAESKRLAQSIQKELVKVLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLL 155

                         170
                  ....*....|....*....
gi 1519253197 350 TDPASRDAIAEAIVVAVKR 368
Cdd:pfam01520 156 NSPAYQQKIAEAIADGILN 174
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 189-367 5.61e-40

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: 139.98  E-value: 5.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 189 RVVIDPSLGGNNRGQVvkGRFGeISEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSRAEIANAFGADLMLCLQA 268
Cdd:cd02696     1 TIVIDPGHGGKDPGAV--GNDG-LKEKDINLAIALKLAKLLEAAGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 269 DKYQNEKASGCASFYFGSEVGSSsligELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMPTVEVVVGYLTNPEDVKI 348
Cdd:cd02696    78 NAAPNSSARGAEVYYYSGSSEES----KRLAEAIQKELVKALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKL 153

                         170
                  ....*....|....*....
gi 1519253197 349 LTDPASRDAIAEAIVVAVK 367
Cdd:cd02696   154 LNSPEYQDKIAEAIAEGIL 172
Ami_3 smart00646
Ami_3 domain;
252-366 4.99e-22

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 90.04  E-value: 4.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197  252 AEIANAFGADLMLCLQADKYQNEKASGCASFYFGSevGSSSLIGELLSGFIQREIVARTNLINCGNHGRTWDLLRVTQMP 331
Cdd:smart00646   1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSD--KGAIRESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMP 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1519253197  332 TVEVVVGYLTNPEDVKILTDPASRDAIAEAIVVAV 366
Cdd:smart00646  79 AVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
PRK10319 PRK10319
N-acetylmuramoyl-L-alanine amidase AmiA;
183-377 3.62e-12

N-acetylmuramoyl-L-alanine amidase AmiA;


Pssm-ID: 182376 [Multi-domain]  Cd Length: 287  Bit Score: 66.34  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 183 PRLAGKR-VVIDPSLGGNNRGQVvkGRFGEiSEEELMWDLATRVEGRMIAAGMETIISRPRQDDPSQKSRAEIANAFGAD 261
Cdd:PRK10319   51 KKSGGKRvVMLDPGHGGIDTGAI--GRNGS-KEKHVVLAIAKNVRSILRNHGIDARLTRSGDTFIPLYDRVEIAHKHGAD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 262 LMLCLQADKYQNEKASGcASFYFGSEVGSSSLIGELLSgfiQREIVA-----------------------RTNLIN---- 314
Cdd:PRK10319  128 LFMSIHADGFTNPKAAG-ASVFALSNRGASSAMAKYLS---ERENRAdevagkkatdkdhllqqvlfdlvQTDTIKnslt 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253197 315 CGNH-----------------GRTWDLLRVTQMPTVEVVVGYLTNPEDVKILTDPASRDAIAEAIVVAVKRlYLQEQDDQ 377
Cdd:PRK10319  204 LGSHilkkikpvhklhsrnteQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQKIATAIAEGIIS-YFHWFDNQ 282
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 114-156 8.90e-12

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 59.92  E-value: 8.90e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1519253197 114 ELGFYTDRLDGRFGEETHAALMNYQMNYGLQADGICGPETIRA 156
Cdd:COG3409    24 ALGYYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWAA 66
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
5-80 1.83e-11

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


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 65.35  E-value: 1.83e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519253197   5 LRVGDRSARVAEVRDALARLGFLQGTDKQVSNakgrtfteaekLFDEPLADALKAFQQTRGIIASGVINDPTLRVL 80
Cdd:COG2989   204 LRPGDSDPRVPALRERLAALGDLPADAPSDSD-----------VYDAELVEAVKRFQARHGLKADGVIGPATLAAL 268
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 115-156 1.28e-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: 56.37  E-value: 1.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1519253197 115 LGFYTDRLDGRFGEETHAALMNYQMNYGLQADGICGPETIRA 156
Cdd:pfam01471  15 LGYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAA 56
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 4-82 3.53e-06

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 44.13  E-value: 3.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519253197   4 ILRVGDRSARVAEVRDALARLGFLQGTdkqvsnAKGRtfteaeklFDEPLADALKAFQQTRGIIASGVINDPTLRVLRE 82
Cdd:COG3409     5 TLRLGDSGEDVRELQQRLNALGYYPGP------VDGI--------FGPATEAAVRAFQRANGLPVDGIVGPATWAALRA 69
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 10-80 2.59e-05

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: 41.35  E-value: 2.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519253197  10 RSARVAEVRDALARLGFLQGTdkqvsnakgrtfteAEKLFDEPLADALKAFQQTRGIIASGVINDPTLRVL 80
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP--------------VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
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