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Conserved domains on  [gi|1633233584|gb|QCJ35461|]
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LysM peptidoglycan-binding domain-containing protein [Enterococcus faecalis]

Protein Classification

LysM peptidoglycan-binding domain-containing protein( domain architecture ID 13292210)

LysM peptidoglycan-binding domain-containing protein may bind N-acetylglucosamine in carbohydrates such as chitin, chitio-oligosaccharides and peptidoglycan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
108-607 1.44e-108

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 340.52  E-value: 1.44e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 108 PTTPSTEQPTADSTTPVESGTTDSSVAEITPV--APSATESEAAPAVT-----PDDEVKVPEARVASAQTFSALSPTQSP 180
Cdd:PRK06347   71 KEAPATATPENTTEPTVEPKQTETKEQTKTPEekQPAAKQVEKAPAEPatvsnPDNATSSSTPATYNLLQKSALRSGATV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 181 SEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYL-NGKWLVKKEPF 259
Cdd:PRK06347  151 QSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKF 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 260 RKYPSYMESFQDNAHVL-KTTSFQAGvyYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTPSSG 338
Cdd:PRK06347  231 RKYPSYHQSLEDYAQVIrKGPSWNPN--YYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDSGKTT 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 339 GNTGGGTVNPGTGGSNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNG 418
Cdd:PRK06347  309 GGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKP 388

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 419 GSNNNQSGTNT-------YYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNN 491
Cdd:PRK06347  389 STGTSTSKPSTgtstnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNT 468

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 492 QSGTNTY------YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNN--GGGATT 563
Cdd:PRK06347  469 SKPSTNTntnakvYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNkpSNSTVK 548

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1633233584 564 SYTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVK 607
Cdd:PRK06347  549 TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 627-668 3.60e-15

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


:

Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 69.73  E-value: 3.60e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1633233584 627 HTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
108-607 1.44e-108

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 340.52  E-value: 1.44e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 108 PTTPSTEQPTADSTTPVESGTTDSSVAEITPV--APSATESEAAPAVT-----PDDEVKVPEARVASAQTFSALSPTQSP 180
Cdd:PRK06347   71 KEAPATATPENTTEPTVEPKQTETKEQTKTPEekQPAAKQVEKAPAEPatvsnPDNATSSSTPATYNLLQKSALRSGATV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 181 SEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYL-NGKWLVKKEPF 259
Cdd:PRK06347  151 QSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKF 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 260 RKYPSYMESFQDNAHVL-KTTSFQAGvyYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTPSSG 338
Cdd:PRK06347  231 RKYPSYHQSLEDYAQVIrKGPSWNPN--YYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDSGKTT 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 339 GNTGGGTVNPGTGGSNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNG 418
Cdd:PRK06347  309 GGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKP 388

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 419 GSNNNQSGTNT-------YYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNN 491
Cdd:PRK06347  389 STGTSTSKPSTgtstnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNT 468

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 492 QSGTNTY------YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNN--GGGATT 563
Cdd:PRK06347  469 SKPSTNTntnakvYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNkpSNSTVK 548

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1633233584 564 SYTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVK 607
Cdd:PRK06347  549 TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 111-331 4.23e-56

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 192.11  E-value: 4.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 111 PSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPtqSPSEFIAELARC 190
Cdd:COG1705    62 ASALGGGASALSSAAALALKSAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASA--SPEEFIAKIAPA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYN--GQSVYMDTWEYLNGKWLVKKEPFRKYPSYMES 268
Cdd:COG1705   140 AQKAAKKYGVPASVLIAQAALESGWGKSELDGSPSNNLFGIKAGGSwqGKSVEVTTTEYVNGKAVKIKARFRAYDSYAES 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1633233584 269 FQDNAHVLKTTSfqagvyYYAGAWKsNTSSYRDATAWL-TGRYATDPSYNAKLNNVITAYNLTQ 331
Cdd:COG1705   220 FRDYARLLKNNP------RYAGALA-NAKDYEAFAKALqKAGYATDPKYADKLISIIESYNLTQ 276
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 177-333 2.39e-39

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 141.80  E-value: 2.39e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584  177 TQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQSVYMDTWEYLNGKWLVKK 256
Cdd:smart00047   5 GGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK-KYNNLFGIKGAYDGRPVRMGTLEYLNGGWVTVK 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584  257 EPFRKYPSymESFQDNAHVLKTTSFqagvyYYAGAWKSNtssyrdatAWLTGRYATDPSYNAKLNNVITAYN--LTQYD 333
Cdd:smart00047  84 AAFRGYFG--EKFIDYAYVLRGQNP-----LYKKRWGSN--------ALQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 127-324 6.03e-27

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 111.48  E-value: 6.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 127 GTTDSSVAEITPVAP----SATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQ------------SPSEFIAELARC 190
Cdd:TIGR02541  79 GLADMIVAQLTKGQGnepsEGAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRprgrshaesvpgHPKSFVNSMLPH 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIK--GSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSY 265
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNAdgsPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 266 MESFQDNAHVLKTTSfqagvyYYAGAWKSNtSSYRDATAWLTGRYATDPSYNAKLNNVI 324
Cdd:TIGR02541 239 EEAFSDYARLLNNNP------RYEAVLQQR-SAESFARGLQRAGYATDPRYARKLLQVI 290
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 176-333 6.68e-22

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 96.73  E-value: 6.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 176 PTQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSkAPNYNLFGIK--GSY----NGQSVYMDTWEYLN 249
Cdd:NF038016  156 PRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLT-REDHNYFGIKcfGSPgpiaVGCRSYATFECSPT 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 250 GKWLVKKEPFRKYPSYMESFQDNAHVLKTTSfqagvyYYAGAWKSNTSSYRDATA-WLTGrYATDPSYNAKLNNVITAYN 328
Cdd:NF038016  235 GGCFDTTATFRAYASAADSFRDHGRFLSVNS------RYAPAFAYTDDPDQFAREiHKAG-YATDPTYADKLIGLMKQYN 307


                  ....*
gi 1633233584 329 LTQYD 333
Cdd:NF038016  308 LYQYD 312
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 191-271 1.06e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 89.94  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQsVYMDTWEYlngkwlVKKEPFRKYPSYMESFQ 270
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAK-ESNNLFGIKASWKGK-VAYDTDEV------TVAARFRKYDSVEESIR 75


                  .
gi 1633233584 271 D 271
Cdd:pfam01832  76 D 76
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 627-668 3.60e-15

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


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 69.73  E-value: 3.60e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1633233584 627 HTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
602-668 7.92e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.43  E-value: 7.92e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 602 QTIIVKKGASAGGNASSTNSASG---KRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:COG1388    84 ARYTVKSGDTLSGIARRYGAAAApspVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 429-472 3.83e-14

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: 66.74  E-value: 3.83e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGI-SGDLIFVGQKLIV 472
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 625-668 2.04e-12

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: 61.73  E-value: 2.04e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1633233584 625 KRHTVKSGDSLWGLSMQYGISIQKIKQLNGL-SGDTIYIGQTLKV 668
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
627-668 2.46e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 61.69  E-value: 2.46e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1633233584  627 HTVKSGDSLWGLSMQYGISIQKIKQLNG-LSGDTIYIGQTLKV 668
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
PRK13914 PRK13914
invasion associated endopeptidase;
603-668 6.54e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 39.40  E-value: 6.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633233584 603 TIIVKKGASAGGNASSTnSASGKRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:PRK13914    7 TIAATAGIAVTAFAAPT-IASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
108-607 1.44e-108

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 340.52  E-value: 1.44e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 108 PTTPSTEQPTADSTTPVESGTTDSSVAEITPV--APSATESEAAPAVT-----PDDEVKVPEARVASAQTFSALSPTQSP 180
Cdd:PRK06347   71 KEAPATATPENTTEPTVEPKQTETKEQTKTPEekQPAAKQVEKAPAEPatvsnPDNATSSSTPATYNLLQKSALRSGATV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 181 SEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYL-NGKWLVKKEPF 259
Cdd:PRK06347  151 QSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKF 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 260 RKYPSYMESFQDNAHVL-KTTSFQAGvyYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTPSSG 338
Cdd:PRK06347  231 RKYPSYHQSLEDYAQVIrKGPSWNPN--YYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDSGKTT 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 339 GNTGGGTVNPGTGGSNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNG 418
Cdd:PRK06347  309 GGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKP 388

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 419 GSNNNQSGTNT-------YYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNN 491
Cdd:PRK06347  389 STGTSTSKPSTgtstnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNT 468

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 492 QSGTNTY------YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNN--GGGATT 563
Cdd:PRK06347  469 SKPSTNTntnakvYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNkpSNSTVK 548

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1633233584 564 SYTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVK 607
Cdd:PRK06347  549 TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 111-331 4.23e-56

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 192.11  E-value: 4.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 111 PSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPtqSPSEFIAELARC 190
Cdd:COG1705    62 ASALGGGASALSSAAALALKSAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASA--SPEEFIAKIAPA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYN--GQSVYMDTWEYLNGKWLVKKEPFRKYPSYMES 268
Cdd:COG1705   140 AQKAAKKYGVPASVLIAQAALESGWGKSELDGSPSNNLFGIKAGGSwqGKSVEVTTTEYVNGKAVKIKARFRAYDSYAES 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1633233584 269 FQDNAHVLKTTSfqagvyYYAGAWKsNTSSYRDATAWL-TGRYATDPSYNAKLNNVITAYNLTQ 331
Cdd:COG1705   220 FRDYARLLKNNP------RYAGALA-NAKDYEAFAKALqKAGYATDPKYADKLISIIESYNLTQ 276
PRK08581 PRK08581
amidase domain-containing protein;
131-335 2.18e-44

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 168.43  E-value: 2.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 131 SSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALS--------------PTQSPSEFIAELARCAQPIAQ 196
Cdd:PRK08581  257 ETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTRSTSLFETGPslsnnddsgsfnvvDSKDTRQFIKSIAKDAHRIGQ 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 197 ANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVL 276
Cdd:PRK08581  337 DNDIYASVMIAQAILESDSGQSALAKSPNHNLFGIKGAYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLI 416

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633233584 277 K--TTSFQAgvyYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTP 335
Cdd:PRK08581  417 KngIDGNST---IYKPTWKSEAKSYKDATSHLSKTYATDPNYAKKLNSIIKHYNLTQFDDE 474
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 177-333 2.39e-39

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 141.80  E-value: 2.39e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584  177 TQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQSVYMDTWEYLNGKWLVKK 256
Cdd:smart00047   5 GGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK-KYNNLFGIKGAYDGRPVRMGTLEYLNGGWVTVK 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584  257 EPFRKYPSymESFQDNAHVLKTTSFqagvyYYAGAWKSNtssyrdatAWLTGRYATDPSYNAKLNNVITAYN--LTQYD 333
Cdd:smart00047  84 AAFRGYFG--EKFIDYAYVLRGQNP-----LYKKRWGSN--------ALQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 127-324 6.03e-27

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 111.48  E-value: 6.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 127 GTTDSSVAEITPVAP----SATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQ------------SPSEFIAELARC 190
Cdd:TIGR02541  79 GLADMIVAQLTKGQGnepsEGAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRprgrshaesvpgHPKSFVNSMLPH 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIK--GSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSY 265
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNAdgsPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 266 MESFQDNAHVLKTTSfqagvyYYAGAWKSNtSSYRDATAWLTGRYATDPSYNAKLNNVI 324
Cdd:TIGR02541 239 EEAFSDYARLLNNNP------RYEAVLQQR-SAESFARGLQRAGYATDPRYARKLLQVI 290
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 176-333 6.68e-22

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 96.73  E-value: 6.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 176 PTQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSkAPNYNLFGIK--GSY----NGQSVYMDTWEYLN 249
Cdd:NF038016  156 PRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLT-REDHNYFGIKcfGSPgpiaVGCRSYATFECSPT 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 250 GKWLVKKEPFRKYPSYMESFQDNAHVLKTTSfqagvyYYAGAWKSNTSSYRDATA-WLTGrYATDPSYNAKLNNVITAYN 328
Cdd:NF038016  235 GGCFDTTATFRAYASAADSFRDHGRFLSVNS------RYAPAFAYTDDPDQFAREiHKAG-YATDPTYADKLIGLMKQYN 307


                  ....*
gi 1633233584 329 LTQYD 333
Cdd:NF038016  308 LYQYD 312
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 191-271 1.06e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 89.94  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQsVYMDTWEYlngkwlVKKEPFRKYPSYMESFQ 270
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAK-ESNNLFGIKASWKGK-VAYDTDEV------TVAARFRKYDSVEESIR 75


                  .
gi 1633233584 271 D 271
Cdd:pfam01832  76 D 76
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
126-324 3.64e-18

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 85.70  E-value: 3.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 126 SGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQSPSEFIAELARCAQPIAQANDLYASVM 205
Cdd:PRK05684   98 SPEQSPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPLASDKPLFGSSDDFVARLSPPAQKAAQQSGVPHHLL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 206 MAQAIVESGWGASTLSKA---PNYNLFGIK--GSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTS 280
Cdd:PRK05684  178 LAQAALESGWGQREIRTAdgsPSHNLFGIKadGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNP 257

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1633233584 281 FQAGVyyyagawKSNTSSYRDATAWLTGRYATDPSYNAKLNNVI 324
Cdd:PRK05684  258 RYAAV-------TQAASPEQFARALQDAGYATDPNYARKLVSVI 294
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 182-325 3.71e-17

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 83.26  E-value: 3.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 182 EFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSK---APNYNLFGIKG--SYNGQSVYMDTWEYLNGKWLVKK 256
Cdd:PRK12713  183 DFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHedgSTSYNLFGIKAgaSWKGKVVNVMTTEYVDGVAQKLV 262

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 257 EPFRKYPSYMESFQDNAHVLKTTSFQAGVyyyAGAWKSNTSSYRDATAwltgRYATDPSYNAKLNNVIT 325
Cdd:PRK12713  263 QPFRAYSSYEESFSDYARLIGNSPRYEAV---TQAGNEIEAARRIQEA----GYATDPRYAEKLISIMG 324
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
353-543 8.67e-17

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 78.21  E-value: 8.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 353 SNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNGGSNNNQSGTNTYYT 432
Cdd:COG1388     8 ANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 433 VKSGDTLNKIAAQYGVSVAnlrswngisgdlifvgqklivkkgasgntggsnnggsnnnqsGTNTYYTIKSGDTLNKIAA 512
Cdd:COG1388    88 VKSGDTLSGIARRYGAAAA------------------------------------------PSPVTYTVKKGDTLWSIAR 125

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1633233584 513 QYGVSVANLRSWNGISGDLIFAGQKIIVKKG 543
Cdd:COG1388   126 RYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 431-473 2.54e-15

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


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 70.12  E-value: 2.54e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1633233584 431 YTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVK 473
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 ...
 627-668 3.60e-15

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


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 69.73  E-value: 3.60e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1633233584 627 HTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
144-320 4.21e-15

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 77.70  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 144 TESEAAPAVTPDDevkvpearVASAQTFSALSPTQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA 223
Cdd:PRK12711  187 AASDAADANAAVN--------ASAASTAAASLGERTPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGNG 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 224 PN-YNLFGIKGS-YNGQSVYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTSfqagvyYYAGAWKSNTSSYRD 301
Cdd:PRK12711  259 GDsNNLFGIKATgWNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNS------RYQQALQAGTDIKGF 332

                         170
                  ....*....|....*....
gi 1633233584 302 ATAWLTGRYATDPSYNAKL 320
Cdd:PRK12711  333 ARGLQQAGYATDPGYAAKI 351
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
429-609 6.99e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.43  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNNQSGTNTYYTIKSGDTLN 508
Cdd:COG1388    16 VLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 509 KIAAQYGVSVAnlrswngisgdlifagqkiivkkgansgstntnkptnnggGATTSYTIKSGDTLNKISAQFGVSVANLR 588
Cdd:COG1388    96 GIARRYGAAAA----------------------------------------PSPVTYTVKKGDTLWSIARRYGVSVEELK 135

                         170       180
                  ....*....|....*....|.
gi 1633233584 589 SWNGIKGDLIFAGQTIIVKKG 609
Cdd:COG1388   136 RWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 363-405 7.13e-15

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


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 68.58  E-value: 7.13e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1633233584 363 YTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVK 405
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
602-668 7.92e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.43  E-value: 7.92e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 602 QTIIVKKGASAGGNASSTNSASG---KRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:COG1388    84 ARYTVKSGDTLSGIARRYGAAAApspVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 172-320 9.79e-15

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 75.73  E-value: 9.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 172 SALSP-------TQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIKGS--YNGQS 239
Cdd:PRK12709  158 SALTPplkgnggSPDADAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGAdgsTSYNVFGIKATkgWTGRT 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 240 VYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTSFQAGVyyyagawksnTSSYRDATAWLTGR----YATDPS 315
Cdd:PRK12709  238 VSAVTTEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRYAGV----------LNASRSVEGFAHGMqkagYATDPH 307


                  ....*
gi 1633233584 316 YNAKL 320
Cdd:PRK12709  308 YAKKL 312
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 354-470 2.04e-14

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 75.93  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 354 NNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNGGsnnnqsgtnTYYTV 433
Cdd:PRK10783  337 DNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDS---------ITYRV 407

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1633233584 434 KSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKL 470
Cdd:PRK10783  408 RKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 499-541 2.54e-14

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: 67.04  E-value: 2.54e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1633233584 499 YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVK 541
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 429-472 3.83e-14

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: 66.74  E-value: 3.83e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGI-SGDLIFVGQKLIV 472
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
430-472 8.24e-14

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 65.93  E-value: 8.24e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1633233584  430 YYTVKSGDTLNKIAAQYGVSVANLRSWNGISG-DLIFVGQKLIV 472
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 506-666 9.42e-14

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 74.00  E-value: 9.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 506 TLNKIAAQYGVSVANLRSWN-GISGDLIFAG--QKIIV-KKGAN-------SGSTNTNKPT---NNGGGATTSYTIKSGD 571
Cdd:PRK10783  273 ELAQAAEMAGMSLTKLKTFNaGYKRSTTAPSgpHYIMVpKKHADqlreslaSGEIAAVQSTlvaDNTPLNSRSYKVRSGD 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 572 TLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVKKGASAGGNASSTNSASGKrhtVKSGDSLWGLSMQYGISIQKIKQ 651
Cdd:PRK10783  353 TLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDSITYR---VRKGDSLSSIAKRHGVNIKDVMR 429

                         170
                  ....*....|....*
gi 1633233584 652 LNGLSGDTIYIGQTL 666
Cdd:PRK10783  430 WNSDTAKNLQPGDKL 444
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 176-320 9.60e-14

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 73.12  E-value: 9.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 176 PTQSP---SEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIKG--SYNGQSVYMDTWEY 247
Cdd:PRK12712  190 PDDAPahvSAFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHAdgsTTFNVFGIKAgaNWKGRVAEVTTTEY 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1633233584 248 LNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTSFQAGVYYYAGAWKSNTSSYRDAtawltgrYATDPSYNAKL 320
Cdd:PRK12712  270 VDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAG-------YATDPAYGHKL 335
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 361-404 1.43e-13

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: 65.20  E-value: 1.43e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1633233584 361 TYYTVKSGDTLNKIAAQYDVSVANLRSWNGI-SGDLIFVGQKLIV 404
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 431-538 1.50e-13

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 73.23  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 431 YTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGsnnnqsgtnTYYTIKSGDTLNKI 510
Cdd:PRK10783  346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDS---------ITYRVRKGDSLSSI 416

                          90       100
                  ....*....|....*....|....*...
gi 1633233584 511 AAQYGVSVANLRSWNGISGDLIFAGQKI 538
Cdd:PRK10783  417 AKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 565-607 1.91e-13

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: 64.72  E-value: 1.91e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1633233584 565 YTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVK 607
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM smart00257
Lysin motif;
362-404 3.26e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 64.00  E-value: 3.26e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1633233584  362 YYTVKSGDTLNKIAAQYDVSVANLRSWNGISG-DLIFVGQKLIV 404
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
498-540 4.97e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 63.62  E-value: 4.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1633233584  498 YYTIKSGDTLNKIAAQYGVSVANLRSWNGISG-DLIFAGQKIIV 540
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 497-540 5.50e-13

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: 63.66  E-value: 5.50e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1633233584 497 TYYTIKSGDTLNKIAAQYGVSVANLRSWNGI-SGDLIFAGQKIIV 540
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 499-597 9.34e-13

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 70.92  E-value: 9.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 499 YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNkptnnggGATTSYTIKSGDTLNKISA 578
Cdd:PRK10783  346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANN-------SDSITYRVRKGDSLSSIAK 418

                          90       100
                  ....*....|....*....|
gi 1633233584 579 QFGVSVANLRSWN-GIKGDL 597
Cdd:PRK10783  419 RHGVNIKDVMRWNsDTAKNL 438
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 625-668 2.04e-12

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: 61.73  E-value: 2.04e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1633233584 625 KRHTVKSGDSLWGLSMQYGISIQKIKQLNGL-SGDTIYIGQTLKV 668
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
627-668 2.46e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 61.69  E-value: 2.46e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1633233584  627 HTVKSGDSLWGLSMQYGISIQKIKQLNG-LSGDTIYIGQTLKV 668
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
565-606 1.15e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.77  E-value: 1.15e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1633233584  565 YTIKSGDTLNKISAQFGVSVANLRSWNGIKG-DLIFAGQTIIV 606
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 563-606 2.46e-11

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: 58.65  E-value: 2.46e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1633233584 563 TSYTIKSGDTLNKISAQFGVSVANLRSWNGIKG-DLIFAGQTIIV 606
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
PRK13914 PRK13914
invasion associated endopeptidase;
433-668 5.25e-09

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 59.04  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 433 VKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGsnnnqsgtnTYYTIKSGDTLN---- 508
Cdd:PRK13914   32 VEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTEKSVSA---------TWLNVRSGAGVDnsii 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 509 ---KIAAQYGVSVANLRSWNGIS---GDLIFAGQKIIVKKGANSGSTNTNKPTNNgggATTSYTIKSGDTLNKISAQFgv 582
Cdd:PRK13914  103 tsiKGGTKVTVETTESNGWHKITyndGKTGFVNGKYLTDKVTSTPVAPTQEVKKE---TTTQQAAPAAETKTEVKQTT-- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 583 svanlrswngikgdlifAGQTIIVKKGASAGGNASSTNSASgkrHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYI 662
Cdd:PRK13914  178 -----------------QATTPAPKVAETKETPVVDQNATT---HAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYV 237


                  ....*.
gi 1633233584 663 GQTLKV 668
Cdd:PRK13914  238 GQKLAI 243
PRK13914 PRK13914
invasion associated endopeptidase;
429-661 9.91e-09

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 58.27  E-value: 9.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNNQ-----------SGTNT 497
Cdd:PRK13914  200 TTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPKAEVKTEAPAAekqaapvvkenTNTNT 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 498 YYTIKSGDTLNKIAAQYGVSVAnlrSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNNGGGATTSYTIKSGDTlnkiS 577
Cdd:PRK13914  280 ATTEKKETTTQQQTAPKAPTEA---AKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNT----N 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 578 AQFGVSVANLRSwngiKGDLIFAGQTIIVKKGASAGGNASSTNSASGKRHTV--KSGDSLWGLSMQYGISIQKIKQLNGL 655
Cdd:PRK13914  353 ANQGSSNNNSNS----SASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVfaKAGISLPRTSGAQYASTTRISESQAK 428


                  ....*.
gi 1633233584 656 SGDTIY 661
Cdd:PRK13914  429 PGDLVF 434
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 572-669 1.34e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 54.36  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 572 TLNKISAQFGVSVANLRSWN-GIKGDLIFAG--QTIIVKKG-------ASAGGNASST--------NSASGKRHTVKSGD 633
Cdd:PRK10783  273 ELAQAAEMAGMSLTKLKTFNaGYKRSTTAPSgpHYIMVPKKhadqlreSLASGEIAAVqstlvadnTPLNSRSYKVRSGD 352

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1633233584 634 SLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKVG 669
Cdd:PRK10783  353 TLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIG 388
PRK13914 PRK13914
invasion associated endopeptidase;
365-548 1.71e-07

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 54.04  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 365 VKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNGGsnnnqsgtnTYYTVKSGDTLN---- 440
Cdd:PRK13914   32 VEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTEKSVSA---------TWLNVRSGAGVDnsii 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 441 ---KIAAQYGVSVANLRSWNGIS---GDLIFVGQKLI--------------VKKGASGNTGGSNNGGSNNNQSGTN---- 496
Cdd:PRK13914  103 tsiKGGTKVTVETTESNGWHKITyndGKTGFVNGKYLtdkvtstpvaptqeVKKETTTQQAAPAAETKTEVKQTTQattp 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 497 -----------------TYYTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGS 548
Cdd:PRK13914  183 apkvaetketpvvdqnaTTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTAT 251
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 609-668 1.18e-06

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 48.85  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633233584 609 GASAGGNASSTNSASGKRHTVKSGDSLWGLSMQY---GISIQKIKQLNGL---SGDTIYIGQTLKV 668
Cdd:COG1652    94 AEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANRDqikNPDLIYPGQVLRI 159
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 182-331 1.47e-06

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 50.56  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 182 EFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIK-GSYNG-QSVYMDTWEYLNGKWLVKK 256
Cdd:PRK12710  132 DFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTRDAdgsSSNNLFNIKtGSHSEvESIQVKTTEYIADTPIKIN 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1633233584 257 EPFRKYPSYMESFQDNAHVLKTTSfqagVYYYAGAWKSNTSSYrdATAWLTGRYATDPSYNAKLNNVITAYNLTQ 331
Cdd:PRK12710  212 ASFRKYPSIEHSFHDYVSLIKGSE----RYQMALANAENPEIY--VSELNKAGYATDPNYSNKILSIYHGDELNQ 280
PRK13914 PRK13914
invasion associated endopeptidase;
361-408 2.03e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 50.96  E-value: 2.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1633233584 361 TYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGA 408
Cdd:PRK13914  200 TTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTA 247
rne PRK10811
ribonuclease E; Reviewed
 43-224 1.13e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.88  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584   43 PVAllPVTAEATEEQPTNAEVAQAPTTETGLVETPTTETTPGTTEQPTTDSSTTTESTTESSKETPT-----------TP 111
Cdd:PRK10811   846 PVV--RPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVvvetthpeviaAP 923

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584  112 STEQP--TADSTTPVESgttdSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAqtfsalspTQSPSEFIAELAR 189
Cdd:PRK10811   924 VTEQPqvITESDVAVAQ----EVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQ--------PAAPVVAEVAAEV 991

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1633233584  190 CAQPIAQANDLYASVmmAQAIVESGWGASTLSKAP 224
Cdd:PRK10811   992 ETVTAVEPEVAPAQV--PEATVEHNHATAPMTRAP 1024
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 511-606 1.29e-03

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 39.99  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 511 AAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNNGGGATTSYTIKSGDTLNKISAQFGVSVANLRSW 590
Cdd:COG1652    58 GLAAAVAAAAAAAVLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFYGDPARWPEI 137

                          90       100
                  ....*....|....*....|..
gi 1633233584 591 -----NGIKG-DLIFAGQTIIV 606
Cdd:COG1652   138 aeanrDQIKNpDLIYPGQVLRI 159
PHA03247 PHA03247
large tegument protein UL36; Provisional
 108-191 3.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584  108 PTTPSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQSPSEFIAEL 187
Cdd:PHA03247  2733 PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812


                   ....
gi 1633233584  188 ARCA 191
Cdd:PHA03247  2813 APAA 2816
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 429-472 3.15e-03

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 38.83  E-value: 3.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1633233584 429 TYYTVKSGDTLNKIAAQ-YGvsvaNLRSWNGI---------SGDLIFVGQKLIV 472
Cdd:COG1652   110 KTYTVKPGDTLWGIAKRfYG----DPARWPEIaeanrdqikNPDLIYPGQVLRI 159
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 501-538 3.83e-03

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 35.54  E-value: 3.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1633233584 501 IKSGDTLNKIAAQYGVSVANLRSWNG-ISG-DLIFAGQKI 538
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPqLSNpNLIYPGMKI 40
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 429-470 5.94e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 37.59  E-value: 5.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1633233584 429 TYYTVKSGDTLNKIA-AQYGvsvaNLRSWNGI---------SGDLIFVGQKL 470
Cdd:PRK11198   96 QFYTVKSGDTLSAIAkKVYG----NANKYNKIfeankpmlkSPDKIYPGQVL 143
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 433-470 6.08e-03

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 35.16  E-value: 6.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1633233584 433 VKSGDTLNKIAAQYGVSVANLRSWNG-ISG-DLIFVGQKL 470
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPqLSNpNLIYPGMKI 40
PRK13914 PRK13914
invasion associated endopeptidase;
603-668 6.54e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 39.40  E-value: 6.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633233584 603 TIIVKKGASAGGNASSTnSASGKRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:PRK13914    7 TIAATAGIAVTAFAAPT-IASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 353-404 6.80e-03

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 38.06  E-value: 6.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1633233584 353 SNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSW-----NGISG-DLIFVGQKLIV 404
Cdd:COG1652   102 AELAPDAPKTYTVKPGDTLWGIAKRFYGDPARWPEIaeanrDQIKNpDLIYPGQVLRI 159
PRK10856 PRK10856
cytoskeleton protein RodZ;
110-206 9.57e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 38.85  E-value: 9.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 110 TPSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQSPsefiAELAR 189
Cdd:PRK10856  168 TTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLP----TDQAG 243

                          90
                  ....*....|....*..
gi 1633233584 190 CAQPIAQANDLyasVMM 206
Cdd:PRK10856  244 VSTPAADPNAL---VMN 257
 
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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