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Conserved domains on  [gi|873897285|ref|WP_048603726|]
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LysM peptidoglycan-binding domain-containing protein [Enterococcus massiliensis]

Protein Classification

muramidase family protein( domain architecture ID 13291719)

muramidase family protein similar to Enterococcus hirae muramidase hydrolyzes the same bond as hen egg-white lysozyme; it is synthesized as a zymogen and requires protease activation

CATH:  3.10.350.10
Gene Ontology:  GO:0097367
PubMed:  18430080|24652063
SCOP:  4000905

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;
67-531 5.01e-99

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 313.17  E-value: 5.01e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  67 AFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQAPNYNLFGIKGSYNGNTVYMNTMEYL-NGKWVTMKEPFR 145
Cdd:PRK06347 152 SFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKFR 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 146 KYPSFKESFADNAYTLRNVYLGGGYYYRGAWKSNTKSYRDATAWLTGRYATAPHYASSLNSVIETYNLTRFDTpasgsag 225
Cdd:PRK06347 232 KYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDS------- 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 226 ggssAGSSNSGNSGSSSSSGSSSSNNSSSSTTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVkngGSS 305
Cdd:PRK06347 305 ----GKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKV---SAG 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 306 SSNTGTGSSNSGSSSSSGASNSNNSSSSTTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVknggSSSS 385
Cdd:PRK06347 378 STTSDTNTSKPSTGTSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV----SAGS 453

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 386 NTGTGSSNSGSSSSSGASNSNNSSSSTSYTVKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVknggtnnSST 465
Cdd:PRK06347 454 TSNTNTSKPSTNTNTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV-------SAG 526

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873897285 466 TTGSSSSSSSSSSASSSASTGGTYTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVK 531
Cdd:PRK06347 527 STTNNTNTAKPSTNKPSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
522-588 2.03e-16

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


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.67  E-value: 2.03e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873897285 522 VYPGQKVTVKKGATASAASTSGSTYKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKVK 588
Cdd:COG1388   88 VKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
67-531 5.01e-99

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 313.17  E-value: 5.01e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  67 AFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQAPNYNLFGIKGSYNGNTVYMNTMEYL-NGKWVTMKEPFR 145
Cdd:PRK06347 152 SFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKFR 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 146 KYPSFKESFADNAYTLRNVYLGGGYYYRGAWKSNTKSYRDATAWLTGRYATAPHYASSLNSVIETYNLTRFDTpasgsag 225
Cdd:PRK06347 232 KYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDS------- 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 226 ggssAGSSNSGNSGSSSSSGSSSSNNSSSSTTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVkngGSS 305
Cdd:PRK06347 305 ----GKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKV---SAG 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 306 SSNTGTGSSNSGSSSSSGASNSNNSSSSTTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVknggSSSS 385
Cdd:PRK06347 378 STTSDTNTSKPSTGTSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV----SAGS 453

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 386 NTGTGSSNSGSSSSSGASNSNNSSSSTSYTVKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVknggtnnSST 465
Cdd:PRK06347 454 TSNTNTSKPSTNTNTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV-------SAG 526

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873897285 466 TTGSSSSSSSSSSASSSASTGGTYTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVK 531
Cdd:PRK06347 527 STTNNTNTAKPSTNKPSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 43-215 2.61e-55

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 188.25  E-value: 2.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  43 MSPLQAEATGTTTNAQMATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQAPNYNLFGIKGSYN- 121
Cdd:COG1705  107 LAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDGSPSNNLFGIKAGGSw 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 122 -GNTVYMNTMEYLNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylggGYYYRGAWKsNTKSYRDATAWL-TGRYATAPH 199
Cdd:COG1705  187 qGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKN-----NPRYAGALA-NAKDYEAFAKALqKAGYATDPK 260

                        170
                 ....*....|....*.
gi 873897285 200 YASSLNSVIETYNLTR 215
Cdd:COG1705  261 YADKLISIIESYNLTQ 276
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 58-217 1.10e-38

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 139.11  E-value: 1.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285    58 QMATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSqAPNYNLFGIKGSYNGNTVYMNTMEYLNGKW 137
Cdd:smart00047   1 KLLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLA-KKYNNLFGIKGAYDGRPVRMGTLEYLNGGW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285   138 VTMKEPFRKYpsFKESFADNAYTLRNVylgggyyyrgawKSNTKSYRDATAWLTGRYATAPHYASSLNSVIETYN--LTR 215
Cdd:smart00047  80 VTVKAAFRGY--FGEKFIDYAYVLRGQ------------NPLYKKRWGSNALQTAGYATDPDYAKKLIRIIALYDekLKG 145


                   ..
gi 873897285   216 FD 217
Cdd:smart00047 146 YD 147
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 63-208 2.61e-24

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: 103.39  E-value: 2.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285   63 SNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQA---PNYNLFGIK--GSYNGNTVYMNTMEYLNGKW 137
Cdd:TIGR02541 146 GHPKSFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNAdgsPSYNLFGIKasGSWQGKVVTTMTTEYVDGVA 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873897285  138 VTMKEPFRKYPSFKESFADNAYTLRNvylgggyyyRGAWKSNTKSyRDATAWLTG----RYATAPHYASSLNSVI 208
Cdd:TIGR02541 226 QKLTAKFRSYSSYEEAFSDYARLLNN---------NPRYEAVLQQ-RSAESFARGlqraGYATDPRYARKLLQVI 290
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 73-213 5.30e-23

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: 93.41  E-value: 5.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285   73 AAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQaPNYNLFGIKGSYNGNtVYMNTMEYlngkwvTMKEPFRKYPSFKE 152
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLAK-ESNNLFGIKASWKGK-VAYDTDEV------TVAARFRKYDSVEE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873897285  153 SFADnaytlrnvylgggyyyrgawksntksyrdatawltgryatapHYASSLNSVIETYNL 213
Cdd:pfam01832  73 SIRD------------------------------------------YYAEKLIAIIERYNL 91
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 60-217 1.12e-18

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: 87.10  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  60 ATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSqAPNYNLFGIK--GSY----NGNTVYmNTMEY- 132
Cdd:NF038016 155 VPRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLT-REDHNYFGIKcfGSPgpiaVGCRSY-ATFECs 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 133 LNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylggGYYYRGAWKSNTKSYRDATA-WLTGrYATAPHYASSLNSVIETY 211
Cdd:NF038016 233 PTGGCFDTTATFRAYASAADSFRDHGRFLSV-----NSRYAPAFAYTDDPDQFAREiHKAG-YATDPTYADKLIGLMKQY 306


                 ....*.
gi 873897285 212 NLTRFD 217
Cdd:NF038016 307 NLYQYD 312
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
522-588 2.03e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.67  E-value: 2.03e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873897285 522 VYPGQKVTVKKGATASAASTSGSTYKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKVK 588
Cdd:COG1388   88 VKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 546-588 3.26e-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: 66.65  E-value: 3.26e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 873897285  546 YKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKVK 588
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 489-588 3.57e-14

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 74.77  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 489 YTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVKKGATASAASTSGS--TYKVKSGDSLWTIAQKYRLTIN 566
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDsiTYRVRKGDSLSSIAKRHGVNIK 425

                         90       100
                 ....*....|....*....|....
gi 873897285 567 QLKSLNQLSSDTILIGQ--TLKVK 588
Cdd:PRK10783 426 DVMRWNSDTAKNLQPGDklTLFVK 449
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 256-299 8.26e-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: 65.58  E-value: 8.26e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 873897285 256 TTYTVKSGDSVWLIANKYGITMNQLIQWNNIKN-NFIYPGQRLVV 299
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
545-587 5.32e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 60.54  E-value: 5.32e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 873897285   545 TYKVKSGDSLWTIAQKYRLTINQLKSLN-QLSSDTILIGQTLKV 587
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNnILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 545-587 8.89e-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: 59.81  E-value: 8.89e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 873897285 545 TYKVKSGDSLWTIAQKYRLTINQLKSLNQLSS-DTILIGQTLKV 587
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
67-531 5.01e-99

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 313.17  E-value: 5.01e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  67 AFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQAPNYNLFGIKGSYNGNTVYMNTMEYL-NGKWVTMKEPFR 145
Cdd:PRK06347 152 SFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKFR 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 146 KYPSFKESFADNAYTLRNVYLGGGYYYRGAWKSNTKSYRDATAWLTGRYATAPHYASSLNSVIETYNLTRFDTpasgsag 225
Cdd:PRK06347 232 KYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDS------- 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 226 ggssAGSSNSGNSGSSSSSGSSSSNNSSSSTTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVkngGSS 305
Cdd:PRK06347 305 ----GKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKV---SAG 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 306 SSNTGTGSSNSGSSSSSGASNSNNSSSSTTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVknggSSSS 385
Cdd:PRK06347 378 STTSDTNTSKPSTGTSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV----SAGS 453

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 386 NTGTGSSNSGSSSSSGASNSNNSSSSTSYTVKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVknggtnnSST 465
Cdd:PRK06347 454 TSNTNTSKPSTNTNTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV-------SAG 526

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873897285 466 TTGSSSSSSSSSSASSSASTGGTYTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVK 531
Cdd:PRK06347 527 STTNNTNTAKPSTNKPSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 43-215 2.61e-55

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 188.25  E-value: 2.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  43 MSPLQAEATGTTTNAQMATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQAPNYNLFGIKGSYN- 121
Cdd:COG1705  107 LAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDGSPSNNLFGIKAGGSw 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 122 -GNTVYMNTMEYLNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylggGYYYRGAWKsNTKSYRDATAWL-TGRYATAPH 199
Cdd:COG1705  187 qGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKN-----NPRYAGALA-NAKDYEAFAKALqKAGYATDPK 260

                        170
                 ....*....|....*.
gi 873897285 200 YASSLNSVIETYNLTR 215
Cdd:COG1705  261 YADKLISIIESYNLTQ 276
PRK08581 PRK08581
amidase domain-containing protein;
63-219 1.53e-46

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 173.05  E-value: 1.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  63 SNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQAPNYNLFGIKGSYNGNTVYMNTMEYLNGKWVTMKE 142
Cdd:PRK08581 318 KDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSPNHNLFGIKGAYEGNSVSFNTLEADGNQLYSINA 397

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873897285 143 PFRKYPSFKESFADNAYTLRNVYLGGGYYYRGAWKSNTKSYRDATAWLTGRYATAPHYASSLNSVIETYNLTRFDTP 219
Cdd:PRK08581 398 GFRKYPSTKESLEDYADLIKNGIDGNSTIYKPTWKSEAKSYKDATSHLSKTYATDPNYAKKLNSIIKHYNLTQFDDE 474
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 58-217 1.10e-38

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 139.11  E-value: 1.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285    58 QMATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSqAPNYNLFGIKGSYNGNTVYMNTMEYLNGKW 137
Cdd:smart00047   1 KLLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLA-KKYNNLFGIKGAYDGRPVRMGTLEYLNGGW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285   138 VTMKEPFRKYpsFKESFADNAYTLRNVylgggyyyrgawKSNTKSYRDATAWLTGRYATAPHYASSLNSVIETYN--LTR 215
Cdd:smart00047  80 VTVKAAFRGY--FGEKFIDYAYVLRGQ------------NPLYKKRWGSNALQTAGYATDPDYAKKLIRIIALYDekLKG 145


                   ..
gi 873897285   216 FD 217
Cdd:smart00047 146 YD 147
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 63-208 2.61e-24

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: 103.39  E-value: 2.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285   63 SNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQA---PNYNLFGIK--GSYNGNTVYMNTMEYLNGKW 137
Cdd:TIGR02541 146 GHPKSFVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIRNAdgsPSYNLFGIKasGSWQGKVVTTMTTEYVDGVA 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873897285  138 VTMKEPFRKYPSFKESFADNAYTLRNvylgggyyyRGAWKSNTKSyRDATAWLTG----RYATAPHYASSLNSVI 208
Cdd:TIGR02541 226 QKLTAKFRSYSSYEEAFSDYARLLNN---------NPRYEAVLQQ-RSAESFARGlqraGYATDPRYARKLLQVI 290
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 73-213 5.30e-23

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: 93.41  E-value: 5.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285   73 AAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQaPNYNLFGIKGSYNGNtVYMNTMEYlngkwvTMKEPFRKYPSFKE 152
Cdd:pfam01832   1 APAAIEAAKKYGIPASVLLAQAALESGWGTSRLAK-ESNNLFGIKASWKGK-VAYDTDEV------TVAARFRKYDSVEE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873897285  153 SFADnaytlrnvylgggyyyrgawksntksyrdatawltgryatapHYASSLNSVIETYNL 213
Cdd:pfam01832  73 SIRD------------------------------------------YYAEKLIAIIERYNL 91
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
54-210 2.22e-19

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 89.17  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  54 TTNAQMATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQA---PNYNLFGIK--GSYNGNTVYMN 128
Cdd:PRK05684 141 PLASDKPLFGSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTAdgsPSHNLFGIKadGSWKGPVTEIT 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 129 TMEYLNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylgggYYYRGAWKSNTKSYRDATAWLTGRYATAPHYASSLNSVI 208
Cdd:PRK05684 221 TTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTN------NPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVI 294


                 ..
gi 873897285 209 ET 210
Cdd:PRK05684 295 QQ 296
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 60-217 1.12e-18

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: 87.10  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  60 ATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSqAPNYNLFGIK--GSY----NGNTVYmNTMEY- 132
Cdd:NF038016 155 VPRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLT-REDHNYFGIKcfGSPgpiaVGCRSY-ATFECs 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 133 LNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylggGYYYRGAWKSNTKSYRDATA-WLTGrYATAPHYASSLNSVIETY 211
Cdd:NF038016 233 PTGGCFDTTATFRAYASAADSFRDHGRFLSV-----NSRYAPAFAYTDDPDQFAREiHKAG-YATDPTYADKLIGLMKQY 306


                 ....*.
gi 873897285 212 NLTRFD 217
Cdd:NF038016 307 NLYQYD 312
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
44-207 2.90e-17

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 83.86  E-value: 2.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  44 SPLQAEATGTTTnAQMATRSnPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQAPN-YNLFGIKGS-YN 121
Cdd:PRK12711 196 AAVNASAASTAA-ASLGERT-PEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGNGGDsNNLFGIKATgWN 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 122 GNTVYMNTMEYLNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylggGYYYRGAWKSNTKSYRDATAWLTGRYATAPHYA 201
Cdd:PRK12711 274 GDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKN-----NSRYQQALQAGTDIKGFARGLQQAGYATDPGYA 348


                 ....*.
gi 873897285 202 SSLNSV 207
Cdd:PRK12711 349 AKIAAI 354
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 34-209 6.04e-17

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 82.28  E-value: 6.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  34 TACSVVTPfmsPLQaeatGTTTNAQMatrsnpSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQA---PN 110
Cdd:PRK12709 155 SAGSALTP---PLK----GNGGSPDA------DAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGAdgsTS 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 111 YNLFGIKGS--YNGNTVYMNTMEYLNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylgggyyyRGAWKSNTKSYRDATA 188
Cdd:PRK12709 222 YNVFGIKATkgWTGRTVSAVTTEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKN---------NPRYAGVLNASRSVEG 292

                        170       180
                 ....*....|....*....|....*
gi 873897285 189 WLTGR----YATAPHYASSLNSVIE 209
Cdd:PRK12709 293 FAHGMqkagYATDPHYAKKLISIMQ 317
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
522-588 2.03e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.67  E-value: 2.03e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873897285 522 VYPGQKVTVKKGATASAASTSGSTYKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKVK 588
Cdd:COG1388   88 VKSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
256-300 3.02e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.29  E-value: 3.02e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 873897285 256 TTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVK 300
Cdd:COG1388  110 VTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 68-208 7.47e-16

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 79.02  E-value: 7.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  68 FITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQ---APNYNLFGIKG--SYNGNTVYMNTMEYLNGKWVTMKE 142
Cdd:PRK12713 184 FVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHedgSTSYNLFGIKAgaSWKGKVVNVMTTEYVDGVAQKLVQ 263

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873897285 143 PFRKYPSFKESFADNAYTLRNvyLGGGYYYRGAWKSNTKSYRDATAwltgRYATAPHYASSLNSVI 208
Cdd:PRK12713 264 PFRAYSSYEESFSDYARLIGN--SPRYEAVTQAGNEIEAARRIQEA----GYATDPRYAEKLISIM 323
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 336-378 1.33e-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: 70.50  E-value: 1.33e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 873897285  336 YTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVK 378
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 ...
 258-300 1.33e-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: 70.50  E-value: 1.33e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 873897285  258 YTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVK 300
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
336-378 1.59e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 74.36  E-value: 1.59e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 873897285 336 YTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVK 378
Cdd:COG1388  112 YTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
414-457 3.43e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 73.20  E-value: 3.43e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 873897285 414 YTVKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVKN 457
Cdd:COG1388  112 YTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPA 155
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 414-456 3.82e-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: 69.35  E-value: 3.82e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 873897285  414 YTVKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVK 456
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 ...
 489-531 8.25e-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: 8.25e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 873897285  489 YTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVK 531
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
489-533 1.78e-14

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 71.28  E-value: 1.78e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 873897285 489 YTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVKKG 533
Cdd:COG1388  112 YTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 546-588 3.26e-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: 66.65  E-value: 3.26e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 873897285  546 YKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKVK 588
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 489-588 3.57e-14

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 74.77  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 489 YTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVKKGATASAASTSGS--TYKVKSGDSLWTIAQKYRLTIN 566
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDsiTYRVRKGDSLSSIAKRHGVNIK 425

                         90       100
                 ....*....|....*....|....
gi 873897285 567 QLKSLNQLSSDTILIGQ--TLKVK 588
Cdd:PRK10783 426 DVMRWNSDTAKNLQPGDklTLFVK 449
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 256-299 8.26e-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: 65.58  E-value: 8.26e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 873897285 256 TTYTVKSGDSVWLIANKYGITMNQLIQWNNIKN-NFIYPGQRLVV 299
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 414-538 2.08e-13

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 72.46  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 414 YTVKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVKNggtnnsstttgsssssSSSSSASSSASTGGTYTVKS 493
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGA----------------GSSAQRLANNSDSITYRVRK 409

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 873897285 494 GDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVT--VKKGATASA 538
Cdd:PRK10783 410 GDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKLTlfVKNNSTPDS 456
LysM smart00257
Lysin motif;
257-299 2.14e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 64.39  E-value: 2.14e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 873897285   257 TYTVKSGDSVWLIANKYGITMNQLIQWNNIKN-NFIYPGQRLVV 299
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 336-377 3.47e-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: 64.04  E-value: 3.47e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 873897285 336 YTVKSGDSVWLIANKYGITMNQLIQWNNIKN-NFIYPGQRLVV 377
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 336-453 4.21e-13

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 71.69  E-value: 4.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 336 YTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVknggssssntgtgssnsgsSSSSGASNSNNSSSSTSYT 415
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI-------------------GAGSSAQRLANNSDSITYR 406

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 873897285 416 VKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRL 453
Cdd:PRK10783 407 VRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
LysM smart00257
Lysin motif;
336-377 7.77e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 62.85  E-value: 7.77e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 873897285   336 YTVKSGDSVWLIANKYGITMNQLIQWNNIKN-NFIYPGQRLVV 377
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 414-455 8.52e-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: 62.89  E-value: 8.52e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 873897285 414 YTVKSGDSVWLIANKHGITMNQLIQWNNIKN-NFIYPGQRLVV 455
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 66-163 9.19e-13

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 69.65  E-value: 9.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  66 SAFITEIAAHAQPIANANDLYASVMIAQAIIESGWGTSTLSQA---PNYNLFGIKG--SYNGNTVYMNTMEYLNGKWVTM 140
Cdd:PRK12712 198 SAFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHAdgsTTFNVFGIKAgaNWKGRVAEVTTTEYVDGQPQKV 277

                         90       100
                 ....*....|....*....|...
gi 873897285 141 KEPFRKYPSFKESFADNAYTLRN 163
Cdd:PRK12712 278 RARFRAYGSYDEACADYARLLTS 300
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 489-530 1.79e-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: 1.79e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 873897285 489 YTVKSGDSVWSIANKHGISMDQFRQWNNIKN-DFVYPGQKVTV 530
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
414-455 2.41e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 61.31  E-value: 2.41e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 873897285   414 YTVKSGDSVWLIANKHGITMNQLIQWNNIKN-NFIYPGQRLVV 455
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 256-375 2.99e-12

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 68.99  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 256 TTYTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVknggssssntgtgssnsgsSSSSGASNSNNSSSSTT 335
Cdd:PRK10783 344 RSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI-------------------GAGSSAQRLANNSDSIT 404

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 873897285 336 YTVKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRL 375
Cdd:PRK10783 405 YRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
LysM smart00257
Lysin motif;
489-530 3.71e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 60.92  E-value: 3.71e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 873897285   489 YTVKSGDSVWSIANKHGISMDQFRQWNNIKN-DFVYPGQKVTV 530
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
545-587 5.32e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 60.54  E-value: 5.32e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 873897285   545 TYKVKSGDSLWTIAQKYRLTINQLKSLN-QLSSDTILIGQTLKV 587
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNnILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 545-587 8.89e-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: 59.81  E-value: 8.89e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 873897285 545 TYKVKSGDSLWTIAQKYRLTINQLKSLNQLSS-DTILIGQTLKV 587
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 530-587 8.08e-10

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 61.29  E-value: 8.08e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 873897285 530 VKKGATASAASTSGSTYKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKV 587
Cdd:PRK10783 330 VQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
PRK13914 PRK13914
invasion associated endopeptidase;
416-588 2.24e-08

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 56.73  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 416 VKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVKNGGTNNSSTTTGSSSSSSSSSSASSSASTGGtyTVKSGD 495
Cdd:PRK13914  32 VEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTEKSVSATWLNVRSGAGVDNSIIT--SIKGGT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 496 SVwsiankhGISMDQFRQWNNI-----KNDFV---YPGQKVT---------VKKGAT----------------------- 535
Cdd:PRK13914 110 KV-------TVETTESNGWHKItyndgKTGFVngkYLTDKVTstpvaptqeVKKETTtqqaapaaetktevkqttqattp 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873897285 536 ---------ASAASTSGSTYKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKVK 588
Cdd:PRK13914 183 apkvaetkeTPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIK 244
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 256-299 9.51e-07

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: 49.23  E-value: 9.51e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 873897285 256 TTYTVKSGDSVWLIANKY---GITMNQLIQWN--NIKN-NFIYPGQRLVV 299
Cdd:COG1652  110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNpDLIYPGQVLRI 159
PRK13914 PRK13914
invasion associated endopeptidase;
414-456 9.67e-07

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 51.73  E-value: 9.67e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 873897285 414 YTVKSGDSVWLIANKHGITMNQLIQWNNIKNNFIYPGQRLVVK 456
Cdd:PRK13914 202 HAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIK 244
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 260-299 1.09e-06

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: 45.56  E-value: 1.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 873897285  260 VKSGDSVWLIANKYGITMNQLIQWN-NIKN-NFIYPGQRLVV 299
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANpQLSNpNLIYPGMKIKI 42
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 338-377 1.09e-06

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: 45.56  E-value: 1.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 873897285  338 VKSGDSVWLIANKYGITMNQLIQWN-NIKN-NFIYPGQRLVV 377
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANpQLSNpNLIYPGMKIKI 42
PRK13914 PRK13914
invasion associated endopeptidase;
338-545 1.79e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 50.57  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 338 VKSGDSVWLIANKYGITMNQLIQWNNIKNNFIYPGQRLVVKNGGSSSSNTGTGSSNSGSSSSSGASNSNNSSsstsyTVK 417
Cdd:PRK13914  32 VEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTEKSVSATWLNVRSGAGVDNSIIT-----SIK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 418 SGDSVWLIANK----HGITmnqliqWNNIKNNFI---YPGQRLV---------VKNGGTNNSSTTTGSSSSSSSSSSASS 481
Cdd:PRK13914 107 GGTKVTVETTEsngwHKIT------YNDGKTGFVngkYLTDKVTstpvaptqeVKKETTTQQAAPAAETKTEVKQTTQAT 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873897285 482 SA--------------STGGTYTVKSGDSVWSIANKHGISMDQFRQWNNIKNDFVYPGQKVTVKKGATASAASTSGST 545
Cdd:PRK13914 181 TPapkvaetketpvvdQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPKAEVKT 258
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 491-530 2.17e-06

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: 44.79  E-value: 2.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 873897285  491 VKSGDSVWSIANKHGISMDQFRQWN-NIKN-DFVYPGQKVTV 530
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANpQLSNpNLIYPGMKIKI 42
PRK13914 PRK13914
invasion associated endopeptidase;
535-587 2.77e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 50.19  E-value: 2.77e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 873897285 535 TASAAST--SGSTYKVKSGDSLWTIAQKYRLTINQLKSLNQLSSDTILIGQTLKV 587
Cdd:PRK13914  17 TAFAAPTiaSASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 48-207 4.55e-06

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 48.64  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285  48 AEATGTTTNAQMATRSNPSAFITEIAAHAQPIANANDLYASVMIAQAIIESGWG---TSTLSQAPNYNLFGIK-GSYNG- 122
Cdd:PRK12710 113 TEVSNTKVTNSEESLSVVDDFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGkfvTRDADGSSSNNLFNIKtGSHSEv 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873897285 123 NTVYMNTMEYLNGKWVTMKEPFRKYPSFKESFADNAYTLRNvylGGGYYYRGAWKSNTKSYrdATAWLTGRYATAPHYAS 202
Cdd:PRK12710 193 ESIQVKTTEYIADTPIKINASFRKYPSIEHSFHDYVSLIKG---SERYQMALANAENPEIY--VSELNKAGYATDPNYSN 267


                 ....*
gi 873897285 203 SLNSV 207
Cdd:PRK12710 268 KILSI 272
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 336-377 6.25e-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: 46.54  E-value: 6.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 873897285 336 YTVKSGDSVWLIANKY---GITMNQLIQWN--NIKN-NFIYPGQRLVV 377
Cdd:COG1652  112 YTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNpDLIYPGQVLRI 159
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 414-455 1.04e-05

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: 46.15  E-value: 1.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 873897285 414 YTVKSGDSVWLIANKH---GITMNQLIQWN--NIKN-NFIYPGQRLVV 455
Cdd:COG1652  112 YTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNpDLIYPGQVLRI 159
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 528-587 1.81e-05

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: 45.38  E-value: 1.81e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873897285 528 VTVKKGATASAASTSGSTYKVKSGDSLWTIAQKY-----RLTinQLKSLN--QLSS-DTILIGQTLKV 587
Cdd:COG1652   94 AEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdpaRWP--EIAEANrdQIKNpDLIYPGQVLRI 159
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 489-530 5.27e-05

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: 43.84  E-value: 5.27e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 873897285 489 YTVKSGDSVWSIANKHGISMDQFRQW-----NNIKN-DFVYPGQKVTV 530
Cdd:COG1652  112 YTVKPGDTLWGIAKRFYGDPARWPEIaeanrDQIKNpDLIYPGQVLRI 159
Bax COG2992
Uncharacterized FlgJ-related protein [General function prediction only];
87-116 3.27e-04

Uncharacterized FlgJ-related protein [General function prediction only];


Pssm-ID: 442231  Cd Length: 253  Bit Score: 42.60  E-value: 3.27e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 873897285  87 ASVMIAQAIIESGWGTSTLSQAPNyNLFGI 116
Cdd:COG2992  121 PSLVLAQAANESGWGTSRFAREGN-NLFGQ 149
PRK14125 PRK14125
cell division suppressor protein YneA; Provisional
 490-532 2.73e-03

cell division suppressor protein YneA; Provisional


Pssm-ID: 184523 [Multi-domain]  Cd Length: 103  Bit Score: 37.70  E-value: 2.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 873897285 490 TVKSGDSVWSIAN----KHGISMDQFRQW----NNIKNDFVYPGQKVT--VKK 532
Cdd:PRK14125  40 TVQEGDTLWALADqyagKHHMAKNEFIEWvedvNNLPSGHIKAGDKLVipVLK 92
 
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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