NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|739610317|ref|WP_037467337|]
View 

LysM peptidoglycan-binding domain-containing protein [Shewanella algae]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
mltD super family cl32574
membrane-bound lytic murein transglycosylase D; Provisional
 50-503 3.62e-145

membrane-bound lytic murein transglycosylase D; Provisional


The actual alignment was detected with superfamily member PRK10783:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 424.53  E-value: 3.62e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  50 TDVWQRIRSQLNMPVPDEKLVRQYRQWYINNPRHLEQISERAAPFMYLIVEQIEERKLPMELALLPIVESAFDPFAYSHG 129
Cdd:PRK10783  60 QDLWAFIGDELKMGIPENSRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 130 AASGLWQFTAPMALHFGLEINWWYDGRRDVPAATAAALNMMEYLYDKTGENWLYAIAAYNTGEGRVLNAVKRNRQKGQAT 209
Cdd:PRK10783 140 NAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPT 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 210 DFWSLSLPKETERYVPQLLALADVIKNADKYGINLtPIANEQK-LEVVDVGSQIDLALAARLAGMEVNELQQFNPGFNRW 288
Cdd:PRK10783 220 DFWSLSLPRETKIYVPKMLALSDILKNSKRYGVRL-PTTDESRaLARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRS 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 289 ATAPEGPHKLVLPLDKAKEFEIALASTEpserlnwlrykirkgdslgvIAKkhhtsidvirsvngisgnnivagkhlLIP 368
Cdd:PRK10783 299 TTAPSGPHYIMVPKKHADQLRESLASGE--------------------IAA--------------------------VQS 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 369 VALKDASAyplskeqrlgqnksgKSKRSYQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQLTIWTKASGKSQ 448
Cdd:PRK10783 333 TLVADNTP---------------LNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK-LKVGQTLTIGAGSSAQRL 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 739610317 449 NANAvmRTVKYKVRSGDSLARIASKFNVTVDDLLEWNQlKASKYLQPGQMLTLFV 503
Cdd:PRK10783 397 ANNS--DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTAKNLQPGDKLTLFV 448
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 50-503 3.62e-145

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 424.53  E-value: 3.62e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  50 TDVWQRIRSQLNMPVPDEKLVRQYRQWYINNPRHLEQISERAAPFMYLIVEQIEERKLPMELALLPIVESAFDPFAYSHG 129
Cdd:PRK10783  60 QDLWAFIGDELKMGIPENSRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 130 AASGLWQFTAPMALHFGLEINWWYDGRRDVPAATAAALNMMEYLYDKTGENWLYAIAAYNTGEGRVLNAVKRNRQKGQAT 209
Cdd:PRK10783 140 NAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPT 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 210 DFWSLSLPKETERYVPQLLALADVIKNADKYGINLtPIANEQK-LEVVDVGSQIDLALAARLAGMEVNELQQFNPGFNRW 288
Cdd:PRK10783 220 DFWSLSLPRETKIYVPKMLALSDILKNSKRYGVRL-PTTDESRaLARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRS 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 289 ATAPEGPHKLVLPLDKAKEFEIALASTEpserlnwlrykirkgdslgvIAKkhhtsidvirsvngisgnnivagkhlLIP 368
Cdd:PRK10783 299 TTAPSGPHYIMVPKKHADQLRESLASGE--------------------IAA--------------------------VQS 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 369 VALKDASAyplskeqrlgqnksgKSKRSYQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQLTIWTKASGKSQ 448
Cdd:PRK10783 333 TLVADNTP---------------LNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK-LKVGQTLTIGAGSSAQRL 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 739610317 449 NANAvmRTVKYKVRSGDSLARIASKFNVTVDDLLEWNQlKASKYLQPGQMLTLFV 503
Cdd:PRK10783 397 ANNS--DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTAKNLQPGDKLTLFV 448
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 102-232 1.02e-55

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 182.33  E-value: 1.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 102 IEERKLPMELALLPIVESAFDPFAYSHGAASGLWQFTAPMALHFGLEINWWYDGRRDVPAATAAALNMMEYLYDKTGeNW 181
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFG-DW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739610317 182 LYAIAAYNTGEGRVLNAVKRNRQKGqATDFWSLSLPKETERYVPQLLALAD 232
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGTDK-WEDYYRLYLPAETRRYVPKFLAAKI 129
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 66-237 3.01e-30

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 122.48  E-value: 3.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  66 DEKLVRQYRQWYINNPRH----LEQISERAAPFMYLIVEQIEERKLPME-LALLPIVESAFDPFAYSHGAASGLWQFTAP 140
Cdd:COG4623  232 GGTLARLYERYFGHVKRDtrafLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQLMPA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 141 MALHFGLeinwwyDGRRDVPAATAAALNMMEYLYDK------TGENWLYAIAAYNTGEGRVLNAVKRNRQKGQATDFWSL 214
Cdd:COG4623  312 TAKELGV------DDRLDPEQSIRAGAKYLRWLYDRfpeaidEPDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFD 385

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 739610317 215 S-------------LPKETERYVPQLLALADVIKNA 237
Cdd:COG4623  386 VeksqpkyydtgyaRGRETVNYVPNIRAYYDIYKRL 421
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 108-206 6.82e-23

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 93.53  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  108 PMELALLPIVESAFDPFAYSHGAASGLWQFTAPMALHFGLEINWWYDGRRDVPAATAAALNMMEYLYDKTGENWLYAIAA 187
Cdd:pfam01464  12 PSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGGDLWLALAA 91

                          90
                  ....*....|....*....
gi 739610317  188 YNTGEGRVLNAVKRNRQKG 206
Cdd:pfam01464  92 YNAGPGRVRKWIKNAGAKD 110
LysM smart00257
Lysin motif;
458-501 1.24e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.38  E-value: 1.24e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 739610317   458 KYKVRSGDSLARIASKFNVTVDDLLEWNQLKASKYLQPGQMLTL 501
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 399-439 1.71e-04

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: 39.01  E-value: 1.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 739610317  399 VKSGDSLWQIAKDNGVSVNELVKWNG-ISAKTPLRPGKQLTI 439
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPqLSNPNLIYPGMKIKI 42
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 50-503 3.62e-145

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 424.53  E-value: 3.62e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  50 TDVWQRIRSQLNMPVPDEKLVRQYRQWYINNPRHLEQISERAAPFMYLIVEQIEERKLPMELALLPIVESAFDPFAYSHG 129
Cdd:PRK10783  60 QDLWAFIGDELKMGIPENSRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 130 AASGLWQFTAPMALHFGLEINWWYDGRRDVPAATAAALNMMEYLYDKTGENWLYAIAAYNTGEGRVLNAVKRNRQKGQAT 209
Cdd:PRK10783 140 NAAGIWQIIPSTGRNYGLKQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPT 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 210 DFWSLSLPKETERYVPQLLALADVIKNADKYGINLtPIANEQK-LEVVDVGSQIDLALAARLAGMEVNELQQFNPGFNRW 288
Cdd:PRK10783 220 DFWSLSLPRETKIYVPKMLALSDILKNSKRYGVRL-PTTDESRaLARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRS 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 289 ATAPEGPHKLVLPLDKAKEFEIALASTEpserlnwlrykirkgdslgvIAKkhhtsidvirsvngisgnnivagkhlLIP 368
Cdd:PRK10783 299 TTAPSGPHYIMVPKKHADQLRESLASGE--------------------IAA--------------------------VQS 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 369 VALKDASAyplskeqrlgqnksgKSKRSYQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQLTIWTKASGKSQ 448
Cdd:PRK10783 333 TLVADNTP---------------LNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK-LKVGQTLTIGAGSSAQRL 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 739610317 449 NANAvmRTVKYKVRSGDSLARIASKFNVTVDDLLEWNQlKASKYLQPGQMLTLFV 503
Cdd:PRK10783 397 ANNS--DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNS-DTAKNLQPGDKLTLFV 448
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 102-232 1.02e-55

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 182.33  E-value: 1.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 102 IEERKLPMELALLPIVESAFDPFAYSHGAASGLWQFTAPMALHFGLEINWWYDGRRDVPAATAAALNMMEYLYDKTGeNW 181
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRFG-DW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739610317 182 LYAIAAYNTGEGRVLNAVKRNRQKGqATDFWSLSLPKETERYVPQLLALAD 232
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGTDK-WEDYYRLYLPAETRRYVPKFLAAKI 129
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 66-237 3.01e-30

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 122.48  E-value: 3.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  66 DEKLVRQYRQWYINNPRH----LEQISERAAPFMYLIVEQIEERKLPME-LALLPIVESAFDPFAYSHGAASGLWQFTAP 140
Cdd:COG4623  232 GGTLARLYERYFGHVKRDtrafLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQLMPA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 141 MALHFGLeinwwyDGRRDVPAATAAALNMMEYLYDK------TGENWLYAIAAYNTGEGRVLNAVKRNRQKGQATDFWSL 214
Cdd:COG4623  312 TAKELGV------DDRLDPEQSIRAGAKYLRWLYDRfpeaidEPDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFD 385

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 739610317 215 S-------------LPKETERYVPQLLALADVIKNA 237
Cdd:COG4623  386 VeksqpkyydtgyaRGRETVNYVPNIRAYYDIYKRL 421
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 1-237 3.42e-29

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 115.48  E-value: 3.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317   1 MLAGSLSLLGGCQLLSQAPESTAEAPVKATPAPVITQAPQVISEPEVAVTDVWQRIRSQLNMPVPDEKLVRQYRQWYINN 80
Cdd:COG0741   10 ALALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAEL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  81 PRHLEQISERAAPFMYLIVEQIEERKLPMELAL-LPIVESAFDPFAYSHGAASGLWQFTAPMALHFGLEIN--WWYDGRR 157
Cdd:COG0741   90 LALAALLLRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGlgPSPDDLF 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 158 DVPAATAAALNMMEYLYDKTGENWLYAIAAYNTGEGRVLNAVKRNRqkgqaTDFWSlSLP-KETERYVPQLLALADVIKN 236
Cdd:COG0741  170 DPETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNG-----DRDGE-IIPyAETRNYVKKVLANYAIYRA 243


                 .
gi 739610317 237 A 237
Cdd:COG0741  244 G 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 108-206 6.82e-23

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 93.53  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  108 PMELALLPIVESAFDPFAYSHGAASGLWQFTAPMALHFGLEINWWYDGRRDVPAATAAALNMMEYLYDKTGENWLYAIAA 187
Cdd:pfam01464  12 PSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQYGGDLWLALAA 91

                          90
                  ....*....|....*....
gi 739610317  188 YNTGEGRVLNAVKRNRQKG 206
Cdd:pfam01464  92 YNAGPGRVRKWIKNAGAKD 110
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
317-501 2.64e-21

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 97.46  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 317 PSERLNWLRYKIRKGDSLGVIAKKHHTSIDVIRSVNGISGNNIVAGKHLliPVALKDASAYPLSK-----EQRLGQNKSG 391
Cdd:PRK06347 399 TGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKL--KVSAGSTSNTNTSKpstntNTSKPSTNTN 476

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 392 KSKRSYQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQL-------TIWTKASGKSQN--ANAVMRTvkYKVR 462
Cdd:PRK06347 477 TNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDF-IYPGQKLkvsagstTNNTNTAKPSTNkpSNSTVKT--YTVK 553

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 739610317 463 SGDSLARIASKFNVTVDDLLEWNQLkASKYLQPGQMLTL 501
Cdd:PRK06347 554 KGDSLWAISRQYKTTVDNIKAWNKL-TSNMIHVGQKLTI 591
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
241-442 3.90e-21

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 90.15  E-value: 3.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 241 GINLTPIANEQKLEVVDVGSQIDLALAARLAGMEVNELQQFNPGFNRWATAPEGPHKLVLPLDKAKEFEIALASTEPSER 320
Cdd:COG1388    1 GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 321 LNWLRYKIRKGDSLGVIAKKHHTSidvirsvngisgnnivagkhllipvalkdasayplskeqrlgqnkSGKSKRSYQVK 400
Cdd:COG1388   81 AAAARYTVKSGDTLSGIARRYGAA---------------------------------------------AAPSPVTYTVK 115

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 739610317 401 SGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQLTIWTK 442
Cdd:COG1388  116 KGDTLWSIARRYGVSVEELKRWNGLSSDT-IRPGQKLKIPAS 156
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
386-499 1.65e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 76.27  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 386 GQNKSGKSKRSYQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQLTIW-------TKASGKSQNANAVMRTVK 458
Cdd:PRK06347 322 SNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDF-IYPGQKLKVSagsttsdTNTSKPSTGTSTSKPSTG 400

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 739610317 459 -------YKVRSGDSLARIASKFNVTVDDLLEWNQLKaSKYLQPGQML 499
Cdd:PRK06347 401 tstnakvYTVVKGDSLWRIANNNKVTIANLKSWNNLK-SDFIYPGQKL 447
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
446-501 2.32e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 67.81  E-value: 2.32e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 739610317 446 KSQNANAVMRTVKYKVRSGDSLARIASKFNVTVDDLLEWNQLKaSKYLQPGQMLTL 501
Cdd:COG1388   99 RRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLS-SDTIRPGQKLKI 153
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 395-439 2.45e-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: 2.45e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 739610317 395 RSYQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTPLRPGKQLTI 439
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 459-501 3.81e-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: 3.81e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 739610317 459 YKVRSGDSLARIASKFNVTVDDLLEWNQLKASKYLQPGQMLTL 501
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 117-229 2.46e-12

lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381594 [Multi-domain]  Cd Length: 111  Bit Score: 63.39  E-value: 2.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 117 VESAFDPFAYSHGAASGLWQFTAPMALHFGLEIN-WWYDGRRDVPAATAaalnMMEYLYDKTGENWLYAIAAYNTGEGRV 195
Cdd:cd00254   10 VESGFNPRAVSPAGARGLMQLMPGTARDLGRRGVdDLFDPEENIRAGAR----YLRELLDRFGGDLELALAAYNAGPGAV 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 739610317 196 LNAVKRNRQkgqatdfwslsLPKETERYVPQLLA 229
Cdd:cd00254   86 DRWGGGEVP-----------PYKETRNYVQRVLA 108
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 459-501 2.60e-12

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


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 61.26  E-value: 2.60e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 739610317  459 YKVRSGDSLARIASKFNVTVDDLLEWNQLKaSKYLQPGQMLTL 501
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLS-SPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
458-501 1.24e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.38  E-value: 1.24e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 739610317   458 KYKVRSGDSLARIASKFNVTVDDLLEWNQLKASKYLQPGQMLTL 501
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 397-440 1.51e-11

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: 58.95  E-value: 1.51e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 739610317  397 YQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQLTIW 440
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKIP 43
LysM smart00257
Lysin motif;
397-439 6.28e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.46  E-value: 6.28e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 739610317   397 YQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTPLRPGKQLTI 439
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 326-368 9.87e-11

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: 56.64  E-value: 9.87e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 739610317  326 YKIRKGDSLGVIAKKHHTSIDVIRSVNGISGNNIVAGKHLLIP 368
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 93-224 3.22e-10

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 58.64  E-value: 3.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  93 PFMYLIVEQIEERKLPMELaLLPIV--ESAFDPFAYSHGAASGLWQFTAPMALHFGLEINWWYDGRRDVpaaTAAALNM- 169
Cdd:cd13401    5 PYRDLVERAAKKNGLDPAL-VYAIIrqESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDL---FDPEYNIr 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739610317 170 -----MEYLYDKTGENWLYAIAAYNTGEGRVLNAVKRNRQkgQATDFWSLSLP-KETERYV 224
Cdd:cd13401   81 lgsayLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRRGD--LDPDLWIETIPfSETRNYV 139
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 117-199 2.53e-09

Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381602 [Multi-domain]  Cd Length: 108  Bit Score: 54.62  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 117 VESAFDPFAY-SHGAASGLWQFTAPMALHFGLEINwwYDGRRDVPAATAAALNMMEYLY-------DKTGENWLYAIAAY 188
Cdd:cd13399   14 VESGFGPNAGgSPAGAQGIAQFMPSTWKAYGVDGN--GDGKADPFNPEDAIASAANYLCrhgwdlnAFLGEDNFLALAAY 91

                         90
                 ....*....|.
gi 739610317 189 NTGEGRVLNAV 199
Cdd:cd13399   92 NAGPGAYANAV 102
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 117-205 8.80e-09

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 54.49  E-value: 8.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 117 VESAFDPFAYSHGAASGLWQFTAPMAlhfGLEINWWYDGRRDVPAAtaaalnmmEYLYD-----KTGENWLY-------- 183
Cdd:cd16893   23 TESSFNPYAVSHSPAYGLMQIVPSTA---GRDVYRLLGGKGGLPSK--------SYLFDpenniDIGTAYLHilqnrylk 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 739610317 184 -----------AIAAYNTGEGRVLNAVKRNRQK 205
Cdd:cd16893   92 giknpksreycAIAAYNGGAGNVLRTFSSDRKK 124
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 326-367 1.62e-07

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: 47.48  E-value: 1.62e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 739610317 326 YKIRKGDSLGVIAKKHHTSIDVIRSVNGISGNN-IVAGKHLLI 367
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
441-499 4.70e-07

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 52.39  E-value: 4.70e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739610317 441 TKASGKSQNANAVMRTVKYKVRSGDSLARIASKFNVTVDDLLEWNQLKaSKYLQPGQML 499
Cdd:PRK06347 315 TGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLK-SDFIYPGQKL 372
LysM smart00257
Lysin motif;
326-367 1.85e-06

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 44.74  E-value: 1.85e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 739610317   326 YKIRKGDSLGVIAKKHHTSIDVIRSVNGISG-NNIVAGKHLLI 367
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 93-224 5.40e-06

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 46.35  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  93 PFMY--LIVEQIEERKLPMELALLPI-VESAFDPFAYSHGAASGLWQF---TAPMAL-HFGLEINW-------------- 151
Cdd:cd16896    1 PLKYreYIEKYAKEYGVDPLLVAAVIkVESNFNPNAVSSKGAIGLMQImpeTAEWIAeKLGLEDFSeddlydpetnirlg 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739610317 152 -WYdgrrdvpaataaalnmMEYLYDKTGENWLYAIAAYNTGEGRVLNAVKRNRQKGQATDfwSLSLP-KETERYV 224
Cdd:cd16896   81 tWY----------------LSYLLKEFDGNLVLALAAYNAGPGNVDKWLKDGGWSGDGKT--LDQIPfPETRHYV 137
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 118-206 1.82e-05

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 44.83  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 118 ESAFDPFAYSHGAASGLWQFTAPMALHFGLEinwwydGRRDVPAATAAALNMMEYLYDKT------GENWLYAIAAYNTG 191
Cdd:cd13403   22 ESRFNPNARSPAGARGLMQLMPSTARELGVN------DRLDPEQNIHAGAKYLRYLRDRFppdidePDRLKFALAAYNAG 95

                         90
                 ....*....|....*
gi 739610317 192 EGRVLNAVKRNRQKG 206
Cdd:cd13403   96 PGHVRDARRLAKKYG 110
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 366-446 1.16e-04

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 44.66  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317 366 LIPVALKDASAYPlSKEQRLGQNKSGKSKRSYQVKSGDSLWQIAKDNGVS---VNELVKwNGISAK--TPLRPGKQLTIW 440
Cdd:COG3061   42 LVPLALTAEADAP-AAAAPAAPAAPEGEWQEYTVQSGDTLSQIFRRLGLSasdLYALLA-AEGDAKplSRLKPGQELRFQ 119


                 ....*.
gi 739610317 441 TKASGK 446
Cdd:COG3061  120 LDADGQ 125
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 399-439 1.71e-04

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: 39.01  E-value: 1.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 739610317  399 VKSGDSLWQIAKDNGVSVNELVKWNG-ISAKTPLRPGKQLTI 439
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPqLSNPNLIYPGMKIKI 42
PRK13914 PRK13914
invasion associated endopeptidase;
396-456 1.80e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 44.02  E-value: 1.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739610317 396 SYQVKSGDSLWQIAKDNGVSVNELVKWNGISAKTpLRPGKQLTIwtKASGKSQNANAVMRT 456
Cdd:PRK13914 201 THAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI--KQTANTATPKAEVKT 258
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 459-504 1.83e-03

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 40.81  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 739610317 459 YKVRSGDSLARIASKFNVTVDDLLEWNQL----KASKYLQPGQMLTLFVD 504
Cdd:COG3061   72 YTVQSGDTLSQIFRRLGLSASDLYALLAAegdaKPLSRLKPGQELRFQLD 121
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 390-439 3.19e-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: 38.45  E-value: 3.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 739610317 390 SGKSKRSYQVKSGDSLWQIAKD---NGVSVNELVKWNGISAKTP--LRPGKQLTI 439
Cdd:COG1652  105 APDAPKTYTVKPGDTLWGIAKRfygDPARWPEIAEANRDQIKNPdlIYPGQVLRI 159
OapA pfam04225
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the ...
 395-454 3.63e-03

Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the Haemophilus influenzae protein OapA, which is required for the expression of colony opacity, thus opacity- associated protein A. The OapA protein is required for efficient nasopharyngeal mucosal colonization, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhibits high-frequency phase variation. The OapA domain has been shown to bind to peptidoglycan in the E. coli protein YtfB. A screen to identify factors that affect cell division in E. coli discovered that overproducing a fragment of YtfB, including its OapA domain, caused cells to grow as long filaments. OapA domains are commonly associated with other domains that are involved in breaking peptidoglycan cross-links. The OapA domain is distantly related to pfam01476.


Pssm-ID: 427799 [Multi-domain]  Cd Length: 85  Bit Score: 36.56  E-value: 3.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739610317  395 RSYQVKSGDSLWQIAKDNGVS---VNELVKWNGisAKTPL---RPGKQLTIWTKASGK------SQNANAVM 454
Cdd:pfam04225   3 KTYTVPKGDTLAQLFRDNNLPisdVNAMAKVEG--ADKPLsniKSGQLVRIKLNAQGRvdelqiENGAKSVM 72
HTH_26 pfam13443
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ...
 405-486 5.98e-03

Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433211 [Multi-domain]  Cd Length: 63  Bit Score: 35.21  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739610317  405 LWQIAKDNGVSVNELVKWNGISAKTplrpgkqLTIWTKasGKsqnanavMRTVkykvrSGDSLARIASKFNVTVDDLLEW 484
Cdd:pfam13443   2 LRKLMADRGISKSDLARATGISRAT-------LSRLRK--GK-------PKRV-----SLDTLDKICDALGCQPGDLLEY 60


                  ..
gi 739610317  485 NQ 486
Cdd:pfam13443  61 VP 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH