|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
1-482 |
0e+00 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 760.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 1 MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNnEVAAAEK 80
Cdd:PRK13914 1 MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVN-EVAAAEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 81 TEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKAVSTPVAPTQEVKKETT 160
Cdd:PRK13914 80 TEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKVTSTPVAPTQEVKKETT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 161 TQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 240
Cdd:PRK13914 160 TQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 241 KLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPAPSTNTNANKTNT 320
Cdd:PRK13914 240 KLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 321 NTNTNTNNTNTNTPSKNTNTNSNTNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 400
Cdd:PRK13914 320 NTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 401 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 480
Cdd:PRK13914 400 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 479
|
..
gi 1071507245 481 RV 482
Cdd:PRK13914 480 RV 481
|
|
| NLPC_P60 |
pfam00877 |
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins. |
379-481 |
2.46e-48 |
|
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
Pssm-ID: 395705 [Multi-domain] Cd Length: 105 Bit Score: 161.68 E-value: 2.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 379 GKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTR-ISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINA 457
Cdd:pfam00877 1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPRSSGQQYNAGKKtIPKSEPQRGDLVFFGTGKGISHVGIYLGNGQMLHA 80
|
90 100
....*....|....*....|....*
gi 1071507245 458 Q-DNGVKYDNIHGSGWGKYLVGFGR 481
Cdd:pfam00877 81 StGGGVSISSLNGGYWQKRLVGVRR 105
|
|
| NlpC |
COG0791 |
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis]; |
268-482 |
1.12e-47 |
|
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440554 [Multi-domain] Cd Length: 218 Bit Score: 164.10 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 268 AAPVVKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTNTPSKNTNTNSNTNTN 347
Cdd:COG0791 1 ASVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSAGAAAAAAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 348 TNSNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQ 427
Cdd:COG0791 81 AGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPRTSADQAAAGTPVSRSE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1071507245 428 AKPGDLVFFD-YGSGISHVGIYVGNGQMINAQD--NGVKYDNIHGSGWGKYLVGFGRV 482
Cdd:COG0791 161 LQPGDLVFFRtGGGGISHVGIYLGNGKFIHASSsgKGVRISSLDSPYWKSRYVGARRV 218
|
|
| wall_hydro_RipC |
NF038345 |
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as ... |
370-462 |
3.75e-21 |
|
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as Mycobacterium tuberculosis, that is activated by conformation change sent as a signal by the cell division-regulating transporter-like complex FtsEX. Members of this family are distinguished from more distant homologs by a Pro/Gly-rich region.
Pssm-ID: 468486 [Multi-domain] Cd Length: 361 Bit Score: 94.80 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 370 IIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFdYgSGISHVGIYV 449
Cdd:NF038345 253 VVQAALTRIGSPYSWGGSGPNAFDCSGLVMWAFQQAGISLPHSSQALARGGQPVSLDDLQPGDVVTF-Y-SDASHAGIYI 330
|
90
....*....|...
gi 1071507245 450 GNGQMINAQDNGV 462
Cdd:NF038345 331 GDGMMVHASTYGT 343
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
201-244 |
3.53e-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: 3.53e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1071507245 201 TTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
202-244 |
1.30e-12 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 62.08 E-value: 1.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1071507245 202 THAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
89-179 |
1.22e-11 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 63.87 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 89 WLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDkavsTPVAPTQ--EVKKETTTQQAAP 166
Cdd:TIGR04211 7 FVYMRSGPGNQYRILGSLKSGTPVTVLERSEDGYSRVRTPKGREGWVLSRYLSD----TPSARERlpELQQELAELQEEL 82
|
90
....*....|...
gi 1071507245 167 aAETKTEVKQTTQ 179
Cdd:TIGR04211 83 -AELQEQLAELRQ 94
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
20-308 |
6.43e-07 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 51.71 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 20 AAPTIASASTVVVeaGDTLwGIAQSKGTTVDAIKKANNLTTDKIVPGQ----KLQVN-NEVAAAEKTEKS---VSATWLN 91
Cdd:NF040676 17 AFTTTATAETIVT--ADVL-NVREKPTTESKVVEKVKNGQELKVINTEdgwsKIELNgKEVFVSSEFTKDvyhVTANLLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 92 VRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNdGKTGFVNGKYLTDKavstpvAPTQEVKKETTTQQAAPAAETK 171
Cdd:NF040676 94 VRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYK-GKTAYANVSFLSST------APTEKKADEKTKQVAKVQKSVK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 172 TEVKQTTQATTPAPKVAETKETPVVDQNATTHAVksgdtiwaLSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKqTANTA 251
Cdd:NF040676 167 AKEEAKTQKVAKAKETTKAQEIVKPKEEVKVQEV--------VKPKEEPKVQEIVKPKEEVKVQEEVKPKEEEK-VQEIV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071507245 252 TPKAEVKTEAPAAEKQAAPV-----VKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPA 308
Cdd:NF040676 238 KPKEEAKVQEEVKVKEEAKVqeiakAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKA 299
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
90-264 |
5.39e-03 |
|
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: 38.95 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 90 LNVRSGAGVDNSIITSIKGGTKVTVETTE-----------SNGWHKItyndGKTGFVNGKYLTdkavSTPVAPTqevkke 158
Cdd:NF038016 1 LNVRSGPATDSAVVGTLANGAKVTVVCKVrgeqirgtvrtTSQWDRL----GSGRYVSHAYVR----WSPSLPT------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 159 tttqQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWalsvkyGVSVQDIMSWNNLSS----S 234
Cdd:NF038016 67 ----CPWCAPKAATVATVTTGGGALNVRAAAGTGAARVGTVANGATVTVECQVW------GQEVDGTGVWYRLGDgryvS 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1071507245 235 SIYV--------GQKLAikqTANTATPKAEVKTEAPAA 264
Cdd:NF038016 137 AAYVrrpwlpwcGQDPP---TVPRGTPAQFIAAVAPPA 171
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
1-482 |
0e+00 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 760.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 1 MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNnEVAAAEK 80
Cdd:PRK13914 1 MNMKKATIAATAGIAVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVN-EVAAAEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 81 TEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKAVSTPVAPTQEVKKETT 160
Cdd:PRK13914 80 TEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKVTSTPVAPTQEVKKETT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 161 TQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 240
Cdd:PRK13914 160 TQQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 241 KLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPAPSTNTNANKTNT 320
Cdd:PRK13914 240 KLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 321 NTNTNTNNTNTNTPSKNTNTNSNTNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 400
Cdd:PRK13914 320 NTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 401 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 480
Cdd:PRK13914 400 VFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINAQDNGVKYDNIHGSGWGKYLVGFG 479
|
..
gi 1071507245 481 RV 482
Cdd:PRK13914 480 RV 481
|
|
| NLPC_P60 |
pfam00877 |
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins. |
379-481 |
2.46e-48 |
|
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
Pssm-ID: 395705 [Multi-domain] Cd Length: 105 Bit Score: 161.68 E-value: 2.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 379 GKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTR-ISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINA 457
Cdd:pfam00877 1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPRSSGQQYNAGKKtIPKSEPQRGDLVFFGTGKGISHVGIYLGNGQMLHA 80
|
90 100
....*....|....*....|....*
gi 1071507245 458 Q-DNGVKYDNIHGSGWGKYLVGFGR 481
Cdd:pfam00877 81 StGGGVSISSLNGGYWQKRLVGVRR 105
|
|
| NlpC |
COG0791 |
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis]; |
268-482 |
1.12e-47 |
|
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440554 [Multi-domain] Cd Length: 218 Bit Score: 164.10 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 268 AAPVVKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTNTPSKNTNTNSNTNTN 347
Cdd:COG0791 1 ASVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSAGAAAAAAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 348 TNSNTNANQGSSNNNSNSSASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQ 427
Cdd:COG0791 81 AGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPRTSADQAAAGTPVSRSE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1071507245 428 AKPGDLVFFD-YGSGISHVGIYVGNGQMINAQD--NGVKYDNIHGSGWGKYLVGFGRV 482
Cdd:COG0791 161 LQPGDLVFFRtGGGGISHVGIYLGNGKFIHASSsgKGVRISSLDSPYWKSRYVGARRV 218
|
|
| wall_hydro_RipC |
NF038345 |
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as ... |
370-462 |
3.75e-21 |
|
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as Mycobacterium tuberculosis, that is activated by conformation change sent as a signal by the cell division-regulating transporter-like complex FtsEX. Members of this family are distinguished from more distant homologs by a Pro/Gly-rich region.
Pssm-ID: 468486 [Multi-domain] Cd Length: 361 Bit Score: 94.80 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 370 IIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFdYgSGISHVGIYV 449
Cdd:NF038345 253 VVQAALTRIGSPYSWGGSGPNAFDCSGLVMWAFQQAGISLPHSSQALARGGQPVSLDDLQPGDVVTF-Y-SDASHAGIYI 330
|
90
....*....|...
gi 1071507245 450 GNGQMINAQDNGV 462
Cdd:NF038345 331 GDGMMVHASTYGT 343
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
23-245 |
5.74e-17 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 83.59 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 23 TIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNNEVAAAEKTEKSVSATWLNVRSGAGVDNSI 102
Cdd:PRK06347 401 TSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNTSKPSTNTNTNAK 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 103 ITSIKGG---------TKVTVETTESngwhkitYNDGKTGFVNgkyltdkavstpvaPTQEVKKetttqqaapAAETKTE 173
Cdd:PRK06347 481 VYTVAKGdslwriannNKVTIANLKS-------WNNLKSDFIY--------------PGQKLKV---------SAGSTTN 530
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071507245 174 VKQTTQATTPAPKVAETKetpvvdqnatTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIK 245
Cdd:PRK06347 531 NTNTAKPSTNKPSNSTVK----------TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
|
|
| YgiM |
COG3103 |
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ... |
77-153 |
8.16e-17 |
|
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];
Pssm-ID: 442337 [Multi-domain] Cd Length: 119 Bit Score: 76.32 E-value: 8.16e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1071507245 77 AAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVeTTESNGWHKITYNDGKTGFVNGKYLTDKAVSTPVAPTQ 153
Cdd:COG3103 1 AAAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTV-LGRSGGWYKVRYSNGKTGWVSSRYLTVTPSARERLPDE 76
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
112-247 |
1.06e-16 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 77.44 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 112 VTVETTESNGWHKITYNDGKTGFVNGKYLTDKAVSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAET- 190
Cdd:COG1388 13 LAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGd 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1071507245 191 -------KETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQT 247
Cdd:COG1388 93 tlsgiarRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
|
|
| spr |
PRK10838 |
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase; |
379-474 |
6.96e-16 |
|
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;
Pssm-ID: 236773 [Multi-domain] Cd Length: 190 Bit Score: 75.96 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 379 GKAYSWGGNGPTTFDCSGYTKYVFAKA-GISLPRTSGAQYASTTRISESQAKPGDLVFFDYGSGISHVGIYVGNGQMINA 457
Cdd:PRK10838 79 GVRYRLGGSTKKGIDCSAFVQRTFREQfGLELPRSTYEQQEMGKSVSRSKLRTGDLVLFRAGSTGRHVGIYIGNNQFVHA 158
|
90
....*....|....*...
gi 1071507245 458 Q-DNGVKYDNIHGSGWGK 474
Cdd:PRK10838 159 StSSGVIISSMNEPYWKK 176
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
25-266 |
1.53e-15 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 78.97 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 25 ASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVN----------NEVAAAEKTEKSVSATWLNVRS 94
Cdd:PRK06347 328 SNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSagsttsdtntSKPSTGTSTSKPSTGTSTNAKV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 95 GAGVDNSIITSIKGGTKVTVETTESngwhkitYNDGKTGFVN-GKYLTDKAVSTpvAPTQEVKKETTTQQAAPAAETKTe 173
Cdd:PRK06347 408 YTVVKGDSLWRIANNNKVTIANLKS-------WNNLKSDFIYpGQKLKVSAGST--SNTNTSKPSTNTNTSKPSTNTNT- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 174 vkqttqattpapkvaetketpvvdqNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQ---TANT 250
Cdd:PRK06347 478 -------------------------NAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAgstTNNT 532
|
250
....*....|....*.
gi 1071507245 251 ATPKAEVKTEAPAAEK 266
Cdd:PRK06347 533 NTAKPSTNKPSNSTVK 548
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
203-245 |
5.18e-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: 5.18e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1071507245 203 HAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIK 245
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
201-244 |
3.53e-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: 3.53e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1071507245 201 TTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
202-244 |
1.30e-12 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 62.08 E-value: 1.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1071507245 202 THAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSS-IYVGQKLAI 244
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
17-71 |
2.29e-12 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 64.73 E-value: 2.29e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1071507245 17 TAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
Cdd:COG1388 99 RRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
30-71 |
2.74e-12 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 60.87 E-value: 2.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1071507245 30 VVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
29-71 |
9.21e-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: 59.42 E-value: 9.21e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1071507245 29 TVVVEAGDTLWGIAQSKGTTVDAIKKANNLTT-DKIVPGQKLQV 71
Cdd:cd00118 2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
89-179 |
1.22e-11 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 63.87 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 89 WLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDkavsTPVAPTQ--EVKKETTTQQAAP 166
Cdd:TIGR04211 7 FVYMRSGPGNQYRILGSLKSGTPVTVLERSEDGYSRVRTPKGREGWVLSRYLSD----TPSARERlpELQQELAELQEEL 82
|
90
....*....|...
gi 1071507245 167 aAETKTEVKQTTQ 179
Cdd:TIGR04211 83 -AELQEQLAELRQ 94
|
|
| SH3b |
smart00287 |
Bacterial SH3 domain homologues; |
80-138 |
7.85e-11 |
|
Bacterial SH3 domain homologues;
Pssm-ID: 214600 [Multi-domain] Cd Length: 63 Bit Score: 57.34 E-value: 7.85e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1071507245 80 KTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGK 138
Cdd:smart00287 1 SETAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYGSGQRGYVPGY 59
|
|
| SH3_3 |
pfam08239 |
Bacterial SH3 domain; |
90-141 |
2.88e-10 |
|
Bacterial SH3 domain;
Pssm-ID: 462405 [Multi-domain] Cd Length: 54 Bit Score: 55.72 E-value: 2.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1071507245 90 LNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLT 141
Cdd:pfam08239 3 LNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGGWYKVRTYDGYEGWVSSSYLS 54
|
|
| YraI |
COG4991 |
Uncharacterized conserved protein YraI [Function unknown]; |
75-151 |
5.12e-10 |
|
Uncharacterized conserved protein YraI [Function unknown];
Pssm-ID: 444015 [Multi-domain] Cd Length: 92 Bit Score: 56.23 E-value: 5.12e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071507245 75 VAAAEKTEKSVSATwLNVRSGAGVDNSIITSIKGGTKVTV-ETTESNGWHKITYnDGKTGFVNGKYLTDKAVSTPVAP 151
Cdd:COG4991 17 PAAAAAATAVATDD-LNLRSGPGTGYPVVGTLPAGATVTVlGCTSGGGWCKVSY-GGQRGWVSARYLQVSYDGQPVPL 92
|
|
| LysM |
smart00257 |
Lysin motif; |
29-71 |
6.45e-10 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 54.37 E-value: 6.45e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1071507245 29 TVVVEAGDTLWGIAQSKGTTVDAIKKANN-LTTDKIVPGQKLQV 71
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
17-95 |
6.94e-09 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 57.82 E-value: 6.94e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1071507245 17 TAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNNEVAAAEKTEKSVSATWlNVRSG 95
Cdd:PRK10783 333 TLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDSITY-RVRKG 410
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
186-244 |
1.31e-07 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 53.97 E-value: 1.31e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071507245 186 KVAETKETPVVD---QNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAI 244
Cdd:PRK10783 326 EIAAVQSTLVADntpLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
20-308 |
6.43e-07 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 51.71 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 20 AAPTIASASTVVVeaGDTLwGIAQSKGTTVDAIKKANNLTTDKIVPGQ----KLQVN-NEVAAAEKTEKS---VSATWLN 91
Cdd:NF040676 17 AFTTTATAETIVT--ADVL-NVREKPTTESKVVEKVKNGQELKVINTEdgwsKIELNgKEVFVSSEFTKDvyhVTANLLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 92 VRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNdGKTGFVNGKYLTDKavstpvAPTQEVKKETTTQQAAPAAETK 171
Cdd:NF040676 94 VRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYK-GKTAYANVSFLSST------APTEKKADEKTKQVAKVQKSVK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 172 TEVKQTTQATTPAPKVAETKETPVVDQNATTHAVksgdtiwaLSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKqTANTA 251
Cdd:NF040676 167 AKEEAKTQKVAKAKETTKAQEIVKPKEEVKVQEV--------VKPKEEPKVQEIVKPKEEVKVQEEVKPKEEEK-VQEIV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071507245 252 TPKAEVKTEAPAAEKQAAPV-----VKENTNTNTATTEKKETATQQQTAPKAPTEAAKPAPA 308
Cdd:NF040676 238 KPKEEAKVQEEVKVKEEAKVqeiakAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKA 299
|
|
| YgiM |
COG3103 |
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ... |
44-135 |
1.04e-05 |
|
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];
Pssm-ID: 442337 [Multi-domain] Cd Length: 119 Bit Score: 44.73 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 44 SKGTTVDAIKKANN---LTTDKivpGQKLQVNNEVAAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVeTTESN 120
Cdd:COG3103 31 PKGEKVTVLGRSGGwykVRYSN---GKTGWVSSRYLTVTPSARERLPDELNLRAGPSTSSEVLGLLPKGETVTV-LKKSG 106
|
90
....*....|....*
gi 1071507245 121 GWHKITYNdgKTGFV 135
Cdd:COG3103 107 GWFKVGYR--GTGWV 119
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
141-308 |
4.36e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.19 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 141 TDKAVSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQ--------ATTPAPKVAE-TKETPVVDQNATTHAVKSGDTI 211
Cdd:PRK10811 867 QPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQpeevvvveTTHPEVIAAPvTEQPQVITESDVAVAQEVAEHA 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 212 WALSVKYGVSVQDimswnnlssssiyvgQKLAIKQTANTATPKAEVKTEAPAAEKQAAPVVKENTNTNTATTEKKETATQ 291
Cdd:PRK10811 947 EPVVEPQDETADI---------------EEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATV 1011
|
170 180
....*....|....*....|..
gi 1071507245 292 QQ---TAP--KAPTEAAKPAPA 308
Cdd:PRK10811 1012 EHnhaTAPmtRAPAPEYVPEAP 1033
|
|
| PRK14125 |
PRK14125 |
cell division suppressor protein YneA; Provisional |
28-69 |
9.84e-05 |
|
cell division suppressor protein YneA; Provisional
Pssm-ID: 184523 [Multi-domain] Cd Length: 103 Bit Score: 41.56 E-value: 9.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1071507245 28 STVVVEAGDTLWGIAQ--------SKGTTVDAIKKANNLTTDKIVPGQKL 69
Cdd:PRK14125 37 VEITVQEGDTLWALADqyagkhhmAKNEFIEWVEDVNNLPSGHIKAGDKL 86
|
|
| spore_safA |
TIGR02899 |
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ... |
205-244 |
1.12e-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: 39.39 E-value: 1.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1071507245 205 VKSGDTIWALSVKYGVSVQDIMSWN-NLSSSS-IYVGQKLAI 244
Cdd:TIGR02899 1 VQKGDTLWKIAKKYGVDFDELIQANpQLSNPNlIYPGMKIKI 42
|
|
| PRK14125 |
PRK14125 |
cell division suppressor protein YneA; Provisional |
205-244 |
3.69e-04 |
|
cell division suppressor protein YneA; Provisional
Pssm-ID: 184523 [Multi-domain] Cd Length: 103 Bit Score: 39.63 E-value: 3.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1071507245 205 VKSGDTIWALSVKY----GVSVQDIMSW----NNLSSSSIYVGQKLAI 244
Cdd:PRK14125 41 VQEGDTLWALADQYagkhHMAKNEFIEWvedvNNLPSGHIKAGDKLVI 88
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
22-71 |
3.70e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 43.14 E-value: 3.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1071507245 22 PTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
Cdd:PRK06347 542 PSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
|
|
| OapA |
COG3061 |
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ... |
159-249 |
5.54e-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: 42.35 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 159 TTTQQAAPAAETKTEVKQTTQATTPAPKVAETKETPvvDQNATTHAVKSGDTIWALSVKYGVSVQDImswNNLSS----- 233
Cdd:COG3061 30 SPDASASRVSQPLVPLALTAEADAPAAAAPAAPAAP--EGEWQEYTVQSGDTLSQIFRRLGLSASDL---YALLAaegda 104
|
90
....*....|....*....
gi 1071507245 234 ---SSIYVGQKLAIKQTAN 249
Cdd:COG3061 105 kplSRLKPGQELRFQLDAD 123
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
25-71 |
5.68e-04 |
|
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: 40.76 E-value: 5.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1071507245 25 ASASTVVVEAGDTLWGIAQS---KGTTVDAIKKANNLT---TDKIVPGQKLQV 71
Cdd:COG1652 107 DAPKTYTVKPGDTLWGIAKRfygDPARWPEIAEANRDQiknPDLIYPGQVLRI 159
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
87-244 |
1.05e-03 |
|
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];
Pssm-ID: 441258 [Multi-domain] Cd Length: 163 Bit Score: 39.99 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 87 ATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNDGKTGFVNGKYLTDKAVSTPVAPTQEVKKETTTQQAAP 166
Cdd:COG1652 4 AAAAAALAALLPAVSAAAATVLALAAAAALAVVAGLGAAVGAGGALAAALPLAAGLAAAVAAAAAAAVLIAPVAVMRAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 167 AAETKTEVKQTTQATTPAPKVAETKetpvvdqnATTHAVKSGDTIWALSVKY---GVSVQDIMSWN--NLSSSS-IYVGQ 240
Cdd:COG1652 84 AAKLSPAVTVAEEAAAPSAELAPDA--------PKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPDlIYPGQ 155
|
....
gi 1071507245 241 KLAI 244
Cdd:COG1652 156 VLRI 159
|
|
| yfaT |
COG3234 |
Uncharacterized conserved protein YfaT, DUF1175 family [Function unknown]; |
426-452 |
4.97e-03 |
|
Uncharacterized conserved protein YfaT, DUF1175 family [Function unknown];
Pssm-ID: 442466 Cd Length: 231 Bit Score: 38.54 E-value: 4.97e-03
10 20
....*....|....*....|....*....
gi 1071507245 426 SQAKPGDLVFFDYGSGIS--HVGIYVGNG 452
Cdd:COG3234 153 NQALPGDLLFFDHPEDDMpyHLMIYMGDG 181
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
141-208 |
5.29e-03 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 39.06 E-value: 5.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071507245 141 TDKAVSTPVAPTQEVKKETTTQ---QAAPAAETKT-EVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSG 208
Cdd:COG3266 292 AAAQPSAVALPAAPAAAAAAAApaeAAAPQPTAAKpVVTETAAPAAPAPEAAAAAAAPAAPAVAKKLAADEQ 363
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
90-264 |
5.39e-03 |
|
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: 38.95 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 90 LNVRSGAGVDNSIITSIKGGTKVTVETTE-----------SNGWHKItyndGKTGFVNGKYLTdkavSTPVAPTqevkke 158
Cdd:NF038016 1 LNVRSGPATDSAVVGTLANGAKVTVVCKVrgeqirgtvrtTSQWDRL----GSGRYVSHAYVR----WSPSLPT------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071507245 159 tttqQAAPAAETKTEVKQTTQATTPAPKVAETKETPVVDQNATTHAVKSGDTIWalsvkyGVSVQDIMSWNNLSS----S 234
Cdd:NF038016 67 ----CPWCAPKAATVATVTTGGGALNVRAAAGTGAARVGTVANGATVTVECQVW------GQEVDGTGVWYRLGDgryvS 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1071507245 235 SIYV--------GQKLAikqTANTATPKAEVKTEAPAA 264
Cdd:NF038016 137 AAYVrrpwlpwcGQDPP---TVPRGTPAQFIAAVAPPA 171
|
|
| |
