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Conserved domains on  [gi|446858559|ref|WP_000935815|]
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N-acetylmuramoyl-L-alanine amidase [Vibrio cholerae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10431 super family cl35918
N-acetylmuramoyl-l-alanine amidase II; Provisional
 15-398 3.01e-102

N-acetylmuramoyl-l-alanine amidase II; Provisional


The actual alignment was detected with superfamily member PRK10431:

Pssm-ID: 236692 [Multi-domain]  Cd Length: 445  Bit Score: 316.03  E-value: 3.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  15 VLLAIAPQTWANVLEGVRVWPSPDETRVVLDVKSEVDYSYFTlSSPERLVVDLKQSTSRAKLPVNVTESGILSKVRASSP 94
Cdd:PRK10431  12 TLLLLCAQAGAATLSDIQVSNGNQQARITLSFIGDPDYAFSH-QSKRTVALDIKQTGVIQGLPLLFSGNNLVKAIRSGTP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  95 PEKSTFRLVFELKQKTTPTLFKlaPTPGGQYGHRLVIDM------PHGKVSESSSASTPSSPAQVSKDA----------- 157
Cdd:PRK10431  91 KDAQTLRLVVDLTENGKTEAVK--RQNGSNYTVVFTINAdvppppPPPPVVAKRVETPAVVAPRVSEPArnpfktesnrt 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 158 ---------------SQLLGNDDIVVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAVPGMKAVLTRRGDYFV 222
Cdd:PRK10431 169 tgvissntvtrpaarATANTGDKVIIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNDDPMFKGVLTRDGDYFI 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 223 NLNKRTEIARRSKAHLLVSVHADAFHTPQPRGGSVFVLNTRRANTEIARWVENHEQQSELLGGAGEVLSKTNNDRNVSQT 302
Cdd:PRK10431 249 SVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLEQHEKQSELLGGAGDVLANSQSDPYLSQA 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 303 LLDLQFSHSQKEGYKVATNILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARAL 382
Cdd:PRK10431 329 VLDLQFGHSQRVGYDVATSVLSQLQRIGELHKRRPEHASLGVLRSPDIPSVLVETGFISNNSEERLLASDDYQQQIAEAI 408

                        410       420
                 ....*....|....*....|
gi 446858559 383 ATAIVQYFEDNP----PEGT 398
Cdd:PRK10431 409 YKGLRNYFLAHPmqsaPQGA 428
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
406-569 5.78e-27

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 115.18  E-value: 5.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 406 AQKHKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTIPASSAPN-----PVPVPVMANP---VETETITHVV 477
Cdd:PRK06347 405 AKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNtntskPSTNTNTSKPstnTNTNAKVYTV 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 478 KTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLKITVSL-----------KDKP----LRKHKVQRGEFLSKIADQ 542
Cdd:PRK06347 485 AKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSttnntntakpsTNKPsnstVKTYTVKKGDSLWAISRQ 564

                        170       180
                 ....*....|....*....|....*..
gi 446858559 543 YNVSVDSIRQANQLRTDQLLVGQQLII 569
Cdd:PRK06347 565 YKTTVDNIKAWNKLTSNMIHVGQKLTI 591
 
Name Accession Description Interval E-value
PRK10431 PRK10431
N-acetylmuramoyl-l-alanine amidase II; Provisional
 15-398 3.01e-102

N-acetylmuramoyl-l-alanine amidase II; Provisional


Pssm-ID: 236692 [Multi-domain]  Cd Length: 445  Bit Score: 316.03  E-value: 3.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  15 VLLAIAPQTWANVLEGVRVWPSPDETRVVLDVKSEVDYSYFTlSSPERLVVDLKQSTSRAKLPVNVTESGILSKVRASSP 94
Cdd:PRK10431  12 TLLLLCAQAGAATLSDIQVSNGNQQARITLSFIGDPDYAFSH-QSKRTVALDIKQTGVIQGLPLLFSGNNLVKAIRSGTP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  95 PEKSTFRLVFELKQKTTPTLFKlaPTPGGQYGHRLVIDM------PHGKVSESSSASTPSSPAQVSKDA----------- 157
Cdd:PRK10431  91 KDAQTLRLVVDLTENGKTEAVK--RQNGSNYTVVFTINAdvppppPPPPVVAKRVETPAVVAPRVSEPArnpfktesnrt 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 158 ---------------SQLLGNDDIVVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAVPGMKAVLTRRGDYFV 222
Cdd:PRK10431 169 tgvissntvtrpaarATANTGDKVIIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNDDPMFKGVLTRDGDYFI 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 223 NLNKRTEIARRSKAHLLVSVHADAFHTPQPRGGSVFVLNTRRANTEIARWVENHEQQSELLGGAGEVLSKTNNDRNVSQT 302
Cdd:PRK10431 249 SVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLEQHEKQSELLGGAGDVLANSQSDPYLSQA 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 303 LLDLQFSHSQKEGYKVATNILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARAL 382
Cdd:PRK10431 329 VLDLQFGHSQRVGYDVATSVLSQLQRIGELHKRRPEHASLGVLRSPDIPSVLVETGFISNNSEERLLASDDYQQQIAEAI 408

                        410       420
                 ....*....|....*....|
gi 446858559 383 ATAIVQYFEDNP----PEGT 398
Cdd:PRK10431 409 YKGLRNYFLAHPmqsaPQGA 428
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
162-392 3.48e-71

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


Pssm-ID: 440621  Cd Length: 204  Bit Score: 227.07  E-value: 3.48e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 162 GNDDIVVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAvPGMKAVLTRRGDYFVNLNKRTEIARRSKAHLLVS 241
Cdd:COG0860   21 PLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEA-PGAKVVLTRDDDTFVSLSERVAIANKAKADLFIS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 242 VHADAFHTPQPRGGSVFVLNTrranteiarwvenheqqsellggagevlsktnndrnvsqtlldlqfSHSQKEGYKVATN 321
Cdd:COG0860  100 IHANAAPNPSARGAEVYYYSG----------------------------------------------SQTSAESKKLAEA 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446858559 322 ILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIVQYFED 392
Cdd:COG0860  134 IQKELVKALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILRYFGK 204
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 167-387 5.42e-60

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: 196.61  E-value: 5.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 167 VVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAvPGMKAVLTRRGDYFVNLNKRTEIARRSKAHLLVSVHADA 246
Cdd:cd02696    1 TIVIDPGHGGKDPGAVGNDGLKEKDINLAIALKLAKLLEA-AGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHANA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 247 FHTPQPRGGSVFVLntrranteiarwvenheqqsellggagevlsktnndrnvsqtlldlqfSHSQKEGYKVATNILREM 326
Cdd:cd02696   80 APNSSARGAEVYYY------------------------------------------------SGSSEESKRLAEAIQKEL 111

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446858559 327 GKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIV 387
Cdd:cd02696  112 VKALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPEYQDKIAEAIAEGIL 172
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 168-386 6.55e-49

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: 167.42  E-value: 6.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  168 VAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAVpGMKAVLTRRGDYFVNLNKRTEIARRSKAHLLVSVHADAF 247
Cdd:pfam01520   1 IVIDPGHGGKDPGAVGPNGILEKDINLKIALKLRKLLEAK-GAEVILTRDSDETVSLEERANIANSNGADLFVSIHANAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  248 HTPQPRGGSVFVLNTRRanteiarwvenheqqsellggagevlsktnndrnvsqtlldlqfshSQKEGYKVATNILREMG 327
Cdd:pfam01520  80 PNSSASGVEVYYLAKRK----------------------------------------------SSAESKRLAQSIQKELV 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446858559  328 KVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAI 386
Cdd:pfam01520 114 KVLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPAYQQKIAEAIADGI 172
spore_cwlD TIGR02883
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of ...
 167-389 1.81e-33

N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]


Pssm-ID: 274337  Cd Length: 189  Bit Score: 125.90  E-value: 1.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  167 VVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAVpGMKAVLTRRGDYFV--------------NLNKRTEIAR 232
Cdd:TIGR02883   2 IIVIDPGHGGIDGGAVGKDGTLEKDITLEIALKLKDYLQEQ-GALVVMTREDDSDLasegtkgysrrkieDLRKRVKLIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  233 RSKAHLLVSVHADAFHTPQPRGGSVFVLNTRRANTEIARWVenheqQSELLggagEVLSKTNNdrnvsqtlldlqfshsq 312
Cdd:TIGR02883  81 ESEADLFISIHLNAFPSSKYSGAQTFYYGNSEENKRLAKFI-----QDELR----RNLDNTNR----------------- 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446858559  313 kegykvatnilremgkvahlhKTEPVNaSLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIVQY 389
Cdd:TIGR02883 135 ---------------------RAKKIN-DYYLLRNAEVPGVIVECGFLSNPEEAELLKDEDYQQKIAAAIYKGVLRY 189
Ami_3 smart00646
Ami_3 domain;
228-386 1.90e-28

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 109.30  E-value: 1.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559   228 TEIARRSKAHLLVSVHADAFHTPQPRGGSVFVLNTRRAnteiarwvenheqqsellggagevlsktnndrnvsqtlldlq 307
Cdd:smart00646   1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGA------------------------------------------ 38

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446858559   308 fshsQKEGYKVATNILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAI 386
Cdd:smart00646  39 ----IRESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMPAVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
406-569 5.78e-27

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 115.18  E-value: 5.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 406 AQKHKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTIPASSAPN-----PVPVPVMANP---VETETITHVV 477
Cdd:PRK06347 405 AKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNtntskPSTNTNTSKPstnTNTNAKVYTV 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 478 KTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLKITVSL-----------KDKP----LRKHKVQRGEFLSKIADQ 542
Cdd:PRK06347 485 AKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSttnntntakpsTNKPsnstVKTYTVKKGDSLWAISRQ 564

                        170       180
                 ....*....|....*....|....*..
gi 446858559 543 YNVSVDSIRQANQLRTDQLLVGQQLII 569
Cdd:PRK06347 565 YKTTVDNIKAWNKLTSNMIHVGQKLTI 591
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
409-572 5.17e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.82  E-value: 5.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 409 HKVQRGESIGLIANQYGVSVDALKKANNLKSSTI----SVGQLLTIPASSAPNPVPVPVMANPVETETITHVVKTGDFLG 484
Cdd:COG1388   16 VLTLLAALLLLAAALAAVALLLLAALAPAGLSLAaalnGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 485 KLATTYKVSVASIKKEnnlksdtlvlgqklkitvslkdkplrkHKVQRGEFLSKIADQYNVSVDSIRQANQLRTDQLLVG 564
Cdd:COG1388   96 GIARRYGAAAAPSPVT---------------------------YTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPG 148


                 ....*...
gi 446858559 565 QQLIIPNK 572
Cdd:COG1388  149 QKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 409-451 1.25e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 62.03  E-value: 1.25e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446858559  409 HKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTIP 451
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 528-569 1.50e-10

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: 56.34  E-value: 1.50e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446858559 528 HKVQRGEFLSKIADQYNVSVDSIRQANQLRTDQLL-VGQQLII 569
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIyPGQKLKI 45
LysM smart00257
Lysin motif;
408-450 1.52e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.60  E-value: 1.52e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 446858559   408 KHKVQRGESIGLIANQYGVSVDALKKANN-LKSSTISVGQLLTI 450
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
PRK10431 PRK10431
N-acetylmuramoyl-l-alanine amidase II; Provisional
 15-398 3.01e-102

N-acetylmuramoyl-l-alanine amidase II; Provisional


Pssm-ID: 236692 [Multi-domain]  Cd Length: 445  Bit Score: 316.03  E-value: 3.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  15 VLLAIAPQTWANVLEGVRVWPSPDETRVVLDVKSEVDYSYFTlSSPERLVVDLKQSTSRAKLPVNVTESGILSKVRASSP 94
Cdd:PRK10431  12 TLLLLCAQAGAATLSDIQVSNGNQQARITLSFIGDPDYAFSH-QSKRTVALDIKQTGVIQGLPLLFSGNNLVKAIRSGTP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  95 PEKSTFRLVFELKQKTTPTLFKlaPTPGGQYGHRLVIDM------PHGKVSESSSASTPSSPAQVSKDA----------- 157
Cdd:PRK10431  91 KDAQTLRLVVDLTENGKTEAVK--RQNGSNYTVVFTINAdvppppPPPPVVAKRVETPAVVAPRVSEPArnpfktesnrt 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 158 ---------------SQLLGNDDIVVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAVPGMKAVLTRRGDYFV 222
Cdd:PRK10431 169 tgvissntvtrpaarATANTGDKVIIAIDAGHGGQDPGAIGPGGTREKNVTIAIARKLRTLLNDDPMFKGVLTRDGDYFI 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 223 NLNKRTEIARRSKAHLLVSVHADAFHTPQPRGGSVFVLNTRRANTEIARWVENHEQQSELLGGAGEVLSKTNNDRNVSQT 302
Cdd:PRK10431 249 SVMGRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMASWLEQHEKQSELLGGAGDVLANSQSDPYLSQA 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 303 LLDLQFSHSQKEGYKVATNILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARAL 382
Cdd:PRK10431 329 VLDLQFGHSQRVGYDVATSVLSQLQRIGELHKRRPEHASLGVLRSPDIPSVLVETGFISNNSEERLLASDDYQQQIAEAI 408

                        410       420
                 ....*....|....*....|
gi 446858559 383 ATAIVQYFEDNP----PEGT 398
Cdd:PRK10431 409 YKGLRNYFLAHPmqsaPQGA 428
AmiC COG0860
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis];
162-392 3.48e-71

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


Pssm-ID: 440621  Cd Length: 204  Bit Score: 227.07  E-value: 3.48e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 162 GNDDIVVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAvPGMKAVLTRRGDYFVNLNKRTEIARRSKAHLLVS 241
Cdd:COG0860   21 PLKGKVIVIDPGHGGKDPGAIGPNGLKEKDVNLDIALRLAELLEA-PGAKVVLTRDDDTFVSLSERVAIANKAKADLFIS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 242 VHADAFHTPQPRGGSVFVLNTrranteiarwvenheqqsellggagevlsktnndrnvsqtlldlqfSHSQKEGYKVATN 321
Cdd:COG0860  100 IHANAAPNPSARGAEVYYYSG----------------------------------------------SQTSAESKKLAEA 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446858559 322 ILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIVQYFED 392
Cdd:COG0860  134 IQKELVKALGLKDRGVKQANFYVLRETDMPAVLVELGFISNPEDEALLKSPAYQQKLAEAIADGILRYFGK 204
MurNAc-LAA cd02696
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ...
 167-387 5.42e-60

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: 196.61  E-value: 5.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 167 VVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAvPGMKAVLTRRGDYFVNLNKRTEIARRSKAHLLVSVHADA 246
Cdd:cd02696    1 TIVIDPGHGGKDPGAVGNDGLKEKDINLAIALKLAKLLEA-AGAKVVLTRDDDTFVSLSERVAIANRAGADLFISIHANA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 247 FHTPQPRGGSVFVLntrranteiarwvenheqqsellggagevlsktnndrnvsqtlldlqfSHSQKEGYKVATNILREM 326
Cdd:cd02696   80 APNSSARGAEVYYY------------------------------------------------SGSSEESKRLAEAIQKEL 111

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446858559 327 GKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIV 387
Cdd:cd02696  112 VKALGLRNRGVKQANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPEYQDKIAEAIAEGIL 172
PRK10319 PRK10319
N-acetylmuramoyl-L-alanine amidase AmiA;
167-392 2.62e-52

N-acetylmuramoyl-L-alanine amidase AmiA;


Pssm-ID: 182376 [Multi-domain]  Cd Length: 287  Bit Score: 180.36  E-value: 2.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 167 VVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAvPGMKAVLTRRGDYFVNLNKRTEIARRSKAHLLVSVHADA 246
Cdd:PRK10319  58 VVMLDPGHGGIDTGAIGRNGSKEKHVVLAIAKNVRSILRN-HGIDARLTRSGDTFIPLYDRVEIAHKHGADLFMSIHADG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 247 FHTPQPRGGSVFVLNTRRANTEIARWVENHEQQSELLGGAgevlSKTNNDRNVSQTLLDLQFSHSQKEGYKVATNILREM 326
Cdd:PRK10319 137 FTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVAGK----KATDKDHLLQQVLFDLVQTDTIKNSLTLGSHILKKI 212

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446858559 327 GKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIVQYFED 392
Cdd:PRK10319 213 KPVHKLHSRNTEQAAFVVLKSPSIPSVLVETSFITNPEEERLLGTTAFRQKIATAIAEGIISYFHW 278
Amidase_3 pfam01520
N-acetylmuramoyl-L-alanine amidase; This enzyme domain cleaves the amide bond between ...
 168-386 6.55e-49

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: 167.42  E-value: 6.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  168 VAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAVpGMKAVLTRRGDYFVNLNKRTEIARRSKAHLLVSVHADAF 247
Cdd:pfam01520   1 IVIDPGHGGKDPGAVGPNGILEKDINLKIALKLRKLLEAK-GAEVILTRDSDETVSLEERANIANSNGADLFVSIHANAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  248 HTPQPRGGSVFVLNTRRanteiarwvenheqqsellggagevlsktnndrnvsqtlldlqfshSQKEGYKVATNILREMG 327
Cdd:pfam01520  80 PNSSASGVEVYYLAKRK----------------------------------------------SSAESKRLAQSIQKELV 113

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446858559  328 KVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAI 386
Cdd:pfam01520 114 KVLGLKNRGVKPANLYVLRNTKMPAVLVELGFISNPEDAKLLNSPAYQQKIAEAIADGI 172
spore_cwlD TIGR02883
N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of ...
 167-389 1.81e-33

N-acetylmuramoyl-L-alanine amidase CwlD; Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]


Pssm-ID: 274337  Cd Length: 189  Bit Score: 125.90  E-value: 1.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  167 VVAIDAGHGGEDPGSIGPTRKYEKDITLSVSKKLADQLNAVpGMKAVLTRRGDYFV--------------NLNKRTEIAR 232
Cdd:TIGR02883   2 IIVIDPGHGGIDGGAVGKDGTLEKDITLEIALKLKDYLQEQ-GALVVMTREDDSDLasegtkgysrrkieDLRKRVKLIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559  233 RSKAHLLVSVHADAFHTPQPRGGSVFVLNTRRANTEIARWVenheqQSELLggagEVLSKTNNdrnvsqtlldlqfshsq 312
Cdd:TIGR02883  81 ESEADLFISIHLNAFPSSKYSGAQTFYYGNSEENKRLAKFI-----QDELR----RNLDNTNR----------------- 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446858559  313 kegykvatnilremgkvahlhKTEPVNaSLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIVQY 389
Cdd:TIGR02883 135 ---------------------RAKKIN-DYYLLRNAEVPGVIVECGFLSNPEEAELLKDEDYQQKIAAAIYKGVLRY 189
Ami_3 smart00646
Ami_3 domain;
228-386 1.90e-28

Ami_3 domain;


Pssm-ID: 214762  Cd Length: 113  Bit Score: 109.30  E-value: 1.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559   228 TEIARRSKAHLLVSVHADAFHTPQPRGGSVFVLNTRRAnteiarwvenheqqsellggagevlsktnndrnvsqtlldlq 307
Cdd:smart00646   1 ANIANAAKADLFVSIHANAGGASAARGFEVYYYSDKGA------------------------------------------ 38

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446858559   308 fshsQKEGYKVATNILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAI 386
Cdd:smart00646  39 ----IRESRALASIIQKSLRKNTGLRDRGVKEANFAVLRETNMPAVLVELGFITNPSDARKLKSAAYQQKLARAIAKGI 113
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
406-569 5.78e-27

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 115.18  E-value: 5.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 406 AQKHKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTIPASSAPN-----PVPVPVMANP---VETETITHVV 477
Cdd:PRK06347 405 AKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNtntskPSTNTNTSKPstnTNTNAKVYTV 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 478 KTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLKITVSL-----------KDKP----LRKHKVQRGEFLSKIADQ 542
Cdd:PRK06347 485 AKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSttnntntakpsTNKPsnstVKTYTVKKGDSLWAISRQ 564

                        170       180
                 ....*....|....*....|....*..
gi 446858559 543 YNVSVDSIRQANQLRTDQLLVGQQLII 569
Cdd:PRK06347 565 YKTTVDNIKAWNKLTSNMIHVGQKLTI 591
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
401-567 5.40e-24

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 106.32  E-value: 5.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 401 ANRGKAQKHKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTIPA--------SSAPNPVPVPVMANP-VETE 471
Cdd:PRK06347 325 GNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAgsttsdtnTSKPSTGTSTSKPSTgTSTN 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 472 TITHVVKTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLKI-----TVSLKDKP----------------LRKHKV 530
Cdd:PRK06347 405 AKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVsagstSNTNTSKPstntntskpstntntnAKVYTV 484

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446858559 531 QRGEFLSKIADQYNVSVDSIRQANQLRTDQLLVGQQL 567
Cdd:PRK06347 485 AKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKL 521
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
310-453 1.14e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 74.75  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 310 HSQKEGYKVATNILREMGKVAHLHKTEPVNASLAVLKSPDIPSVLVETGFISNPSEEKLLIQRSHQDKLARALATAIVQY 389
Cdd:COG1388    7 SANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARY 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 390 FEDNPPEGTLFANRGKAQK------HKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTIPAS 453
Cdd:COG1388   87 TVKSGDTLSGIARRYGAAAapspvtYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
409-572 5.17e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.82  E-value: 5.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 409 HKVQRGESIGLIANQYGVSVDALKKANNLKSSTI----SVGQLLTIPASSAPNPVPVPVMANPVETETITHVVKTGDFLG 484
Cdd:COG1388   16 VLTLLAALLLLAAALAAVALLLLAALAPAGLSLAaalnGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 485 KLATTYKVSVASIKKEnnlksdtlvlgqklkitvslkdkplrkHKVQRGEFLSKIADQYNVSVDSIRQANQLRTDQLLVG 564
Cdd:COG1388   96 GIARRYGAAAAPSPVT---------------------------YTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPG 148


                 ....*...
gi 446858559 565 QQLIIPNK 572
Cdd:COG1388  149 QKLKIPAS 156
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 31-132 9.22e-15

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


Pssm-ID: 463338  Cd Length: 96  Bit Score: 70.03  E-value: 9.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559   31 VRVWPSPDETRVVLDVKSEVDYSYFTLSSPERLVVDLKQSTSRAKLPVNVTESGILSKVRAsSPPEKSTFRLVFELKQKT 110
Cdd:pfam11741   1 VRVWPTDDGTELELETSGGEKYQVFTLSNPNRLVIDIPGAQLGLPLKRIENPSPGIKSVRV-GQFDPNTVRVVVDLDGSV 79

                          90       100
                  ....*....|....*....|..
gi 446858559  111 TPTLfklaptPGGQYGHRLVID 132
Cdd:pfam11741  80 LPQV------PVFKSGEGLVVD 95
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 409-451 1.25e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 62.03  E-value: 1.25e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446858559  409 HKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTIP 451
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 528-570 5.19e-12

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: 60.49  E-value: 5.19e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446858559  528 HKVQRGEFLSKIADQYNVSVDSIRQANQLRTDQLLVGQQLIIP 570
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 368-524 1.24e-11

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 67.07  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 368 LLIQRSHQDKLARALAT---AIVQyfednpPEGTLFANRGKAQKHKVQRGESIGLIANQYGVSVDALKKANNLKSSTISV 444
Cdd:PRK10783 308 IMVPKKHADQLRESLASgeiAAVQ------STLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKV 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 445 GQLLTIPASSAPNpvpvpvmANPVETETITHVVKTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLKITVSLKDKP 524
Cdd:PRK10783 382 GQTLTIGAGSSAQ-------RLANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKLTLFVKNNSTP 454
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 528-569 1.50e-10

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: 56.34  E-value: 1.50e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446858559 528 HKVQRGEFLSKIADQYNVSVDSIRQANQLRTDQLL-VGQQLII 569
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIyPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 407-450 1.79e-10

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: 56.34  E-value: 1.79e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446858559 407 QKHKVQRGESIGLIANQYGVSVDALKKANNLKS-STISVGQLLTI 450
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 475-517 2.51e-10

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: 55.48  E-value: 2.51e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446858559  475 HVVKTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLKIT 517
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM smart00257
Lysin motif;
408-450 1.52e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.60  E-value: 1.52e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 446858559   408 KHKVQRGESIGLIANQYGVSVDALKKANN-LKSSTISVGQLLTI 450
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
527-569 3.07e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.45  E-value: 3.07e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 446858559   527 KHKVQRGEFLSKIADQYNVSVDSIRQAN-QLRTDQLLVGQQLII 569
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNnILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 473-516 3.50e-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: 52.49  E-value: 3.50e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446858559 473 ITHVVKTGDFLGKLATTYKVSVASIKKENNLKS-DTLVLGQKLKI 516
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
474-516 8.58e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 51.29  E-value: 8.58e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 446858559   474 THVVKTGDFLGKLATTYKVSVASIKKENN-LKSDTLVLGQKLKI 516
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 432-567 5.93e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 52.04  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 432 KKANNLKSSTISVGQLLTIPASSAPNpvpvpvmaNPVETETIThvVKTGDFLGKLATTYKVSVASIKKENNLKSDTLVLG 511
Cdd:PRK10783 313 KHADQLRESLASGEIAAVQSTLVADN--------TPLNSRSYK--VRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVG 382

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446858559 512 QKLKITVSLKDKPLRK------HKVQRGEFLSKIADQYNVSVDSIRQANQLRTDQLLVGQQL 567
Cdd:PRK10783 383 QTLTIGAGSSAQRLANnsdsitYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
PRK13914 PRK13914
invasion associated endopeptidase;
449-521 7.93e-07

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 51.73  E-value: 7.93e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446858559 449 TIPASSAPNPVPVPVmanpVETETITHVVKTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLKITVSLK 521
Cdd:PRK13914 180 TTPAPKVAETKETPV----VDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTAN 248
PRK13914 PRK13914
invasion associated endopeptidase;
436-517 4.39e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 49.41  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 436 NLKSSTISvgqlltipassAPNPVPVPVMANPVETETITHVVKTGDFLGKLATTYKVSVASIKKENNLKSDTLVLGQKLK 515
Cdd:PRK13914   2 NMKKATIA-----------ATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQ 70


                 ..
gi 446858559 516 IT 517
Cdd:PRK13914  71 VN 72
PRK13914 PRK13914
invasion associated endopeptidase;
406-507 4.43e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 49.41  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858559 406 AQKHKVQRGESIGLIANQYGVSVDALKKANNLKSSTISVGQLLTI--PASSAPNPVPVPVMANPVETETiTHVVKtgdfl 483
Cdd:PRK13914 199 ATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIkqTANTATPKAEVKTEAPAAEKQA-APVVK----- 272

                         90       100
                 ....*....|....*....|....
gi 446858559 484 gklATTYKVSVASIKKENNLKSDT 507
Cdd:PRK13914 273 ---ENTNTNTATTEKKETTTQQQT 293
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 526-571 1.14e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.73  E-value: 1.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446858559 526 RKHKVQRGEFLSKIADQYNVSVDSIRQANQLRTDQLLVGQQLIIPN 571
Cdd:PRK10783 344 RSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGA 389
AMIN pfam11741
AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the ...
 31-67 1.58e-03

AMIN domain; This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localizes to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localization of periplasmic protein complexes.


Pssm-ID: 463338  Cd Length: 96  Bit Score: 38.05  E-value: 1.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446858559   31 VRVW-PSPDETRVVLDVKSEVDYSYFTLSSPERLVVDL 67
Cdd:pfam11741  59 VRVGqFDPNTVRVVVDLDGSVLPQVPVFKSGEGLVVDL 96
 
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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