|
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
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|
| 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
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