|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11649 |
PRK11649 |
putative peptidase; Provisional |
1-436 |
3.43e-133 |
|
putative peptidase; Provisional
Pssm-ID: 236946 [Multi-domain] Cd Length: 439 Bit Score: 390.57 E-value: 3.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 1 MKRLRPLVAQAANwepPVPRKHFYAMLLLTAMTLsAVAVL----------PAPGDI-LERP-LRLELPIATTgtATNEDN 68
Cdd:PRK11649 1 MQQIARSIALAFN---NLPRPHRVMLGSLTVLTL-AVAVWrpyvyhpesaPIVKTIeLEKSeIRSLLPEASE--PIDQAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 69 TDFNDIPDHELveaavpEDDIPADGTPQwqDYRVRNGENLTTIFNNLGLSTTTLYKVldADAKNNLARLKPGQTIELLID 148
Cdd:PRK11649 75 QEDEAIPQDEL------DDKIAGEAGVH--EYVVSTGDTLSSILNQYGIDMSDISQL--AAQDKELRNLKIGQQLSWTLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 149 QDNILQQLKIRLNIKQTLVLERTDDTYSANMLNEEVEWQQKSYDGVINGSFYVSARNAGIPANHIQKIANLFQWRLNFAK 228
Cdd:PRK11649 145 ADGDLQRLTWEVSRRETRTYDRTGNGFKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEISAVIKALQWQMDFRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 229 dLQRGDKFKVLVRQETVEGKSTgNTQLLGVEVFSQGKTVSAWLSEDGNYYDGQANSLERGFRRYPTHSRYRVSSNFNPAR 308
Cdd:PRK11649 225 -LKKGDEFSVLMSREMLDGKSE-QSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRFPTAKQFRISSNFNPRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 309 RHPITGQVRPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALS 388
Cdd:PRK11649 303 LNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALS 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 759408745 389 GNTGRSTGAHLHYEVRLNNRPVDAMKVKLPMAEPLSGKDKRQFLAKVK 436
Cdd:PRK11649 383 GNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDRREYLAQVK 430
|
|
| OapA |
COG3061 |
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ... |
17-434 |
7.33e-63 |
|
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: 209.14 E-value: 7.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 17 PVPRKHFYAMLLLTAMTLSAVaVLPAPGDILERPLRLELPIATTGTAtnedntdfnDIPdhelveaAVPEDDIPADGTPQ 96
Cdd:COG3061 6 PLPRKHRRLLGLLSALLLLAL-LLPSPDASASRVSQPLVPLALTAEA---------DAP-------AAAAPAAPAAPEGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 97 WQDYRVRNGENLTTIFNNLGLSTTTLYKVLDAD-AKNNLARLKPGQTIELLIDQDNILQQLKIRLNIKQTLVLERTDDTY 175
Cdd:COG3061 69 WQEYTVQSGDTLSQIFRRLGLSASDLYALLAAEgDAKPLSRLKPGQELRFQLDADGQLQALRYEVSRLETLLFTRQGDGF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 176 ------------------SANMLNEEVEWQQKSYDGVINGSFYVSARNAGIPANHIQKIANLFQWRLNFAKDLQRGDKFK 237
Cdd:COG3061 149 qrkrvtelsdgsfsadaaLASLETLELAAAAGILSDFIAAALDAGAGDAGLVELEIILDDDIDFADLLFAADRFTGDYFR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 238 VLVRQETVEGKSTGNTQLLGVEVFSQGKTVSAWLSEDGNYYDGQANSLERGFRRYPTHSRYRVSSNFNPARRHPITGQVR 317
Cdd:COG3061 229 VYAEGEGGDGGYIGAGGFRAAKFRRRAVRFRRSSSSSSYRRRPHRLSRRRRLRRGPDAAAPSGSSNAAGGGGHKITRRGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 318 PHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGNTGRSTGA 397
Cdd:COG3061 309 GGGGAAVGVGTGTPTTGAGLGVVRGGRGGGGGVVVGQIGRGGTYGGTGLHLHKHGHKGGGVVGQGVTIGTLGGTGPTTGP 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 759408745 398 HLHYEVRLNNRPVDAMKVKLPMAEPLSGKDKRQFLAK 434
Cdd:COG3061 389 HLHYEFVQNGVRVAPLTVKLPAAPPLAAAAAAAFKAL 425
|
|
| Peptidase_M23 |
pfam01551 |
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ... |
317-411 |
5.06e-44 |
|
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
Pssm-ID: 460250 [Multi-domain] Cd Length: 96 Bit Score: 149.23 E-value: 5.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 317 RPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGNTGRSTG 396
Cdd:pfam01551 1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80
|
90
....*....|....*
gi 759408745 397 AHLHYEVRLNNRPVD 411
Cdd:pfam01551 81 PHLHFEIRKNGKPVD 95
|
|
| M23_peptidase |
cd12797 |
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ... |
319-403 |
6.87e-39 |
|
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 135.03 E-value: 6.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 319 HEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGNTGRSTGAH 398
Cdd:cd12797 1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80
|
....*
gi 759408745 399 LHYEV 403
Cdd:cd12797 81 LHFEI 85
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11649 |
PRK11649 |
putative peptidase; Provisional |
1-436 |
3.43e-133 |
|
putative peptidase; Provisional
Pssm-ID: 236946 [Multi-domain] Cd Length: 439 Bit Score: 390.57 E-value: 3.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 1 MKRLRPLVAQAANwepPVPRKHFYAMLLLTAMTLsAVAVL----------PAPGDI-LERP-LRLELPIATTgtATNEDN 68
Cdd:PRK11649 1 MQQIARSIALAFN---NLPRPHRVMLGSLTVLTL-AVAVWrpyvyhpesaPIVKTIeLEKSeIRSLLPEASE--PIDQAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 69 TDFNDIPDHELveaavpEDDIPADGTPQwqDYRVRNGENLTTIFNNLGLSTTTLYKVldADAKNNLARLKPGQTIELLID 148
Cdd:PRK11649 75 QEDEAIPQDEL------DDKIAGEAGVH--EYVVSTGDTLSSILNQYGIDMSDISQL--AAQDKELRNLKIGQQLSWTLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 149 QDNILQQLKIRLNIKQTLVLERTDDTYSANMLNEEVEWQQKSYDGVINGSFYVSARNAGIPANHIQKIANLFQWRLNFAK 228
Cdd:PRK11649 145 ADGDLQRLTWEVSRRETRTYDRTGNGFKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEISAVIKALQWQMDFRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 229 dLQRGDKFKVLVRQETVEGKSTgNTQLLGVEVFSQGKTVSAWLSEDGNYYDGQANSLERGFRRYPTHSRYRVSSNFNPAR 308
Cdd:PRK11649 225 -LKKGDEFSVLMSREMLDGKSE-QSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRFPTAKQFRISSNFNPRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 309 RHPITGQVRPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALS 388
Cdd:PRK11649 303 LNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALS 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 759408745 389 GNTGRSTGAHLHYEVRLNNRPVDAMKVKLPMAEPLSGKDKRQFLAKVK 436
Cdd:PRK11649 383 GNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDRREYLAQVK 430
|
|
| OapA |
COG3061 |
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ... |
17-434 |
7.33e-63 |
|
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: 209.14 E-value: 7.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 17 PVPRKHFYAMLLLTAMTLSAVaVLPAPGDILERPLRLELPIATTGTAtnedntdfnDIPdhelveaAVPEDDIPADGTPQ 96
Cdd:COG3061 6 PLPRKHRRLLGLLSALLLLAL-LLPSPDASASRVSQPLVPLALTAEA---------DAP-------AAAAPAAPAAPEGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 97 WQDYRVRNGENLTTIFNNLGLSTTTLYKVLDAD-AKNNLARLKPGQTIELLIDQDNILQQLKIRLNIKQTLVLERTDDTY 175
Cdd:COG3061 69 WQEYTVQSGDTLSQIFRRLGLSASDLYALLAAEgDAKPLSRLKPGQELRFQLDADGQLQALRYEVSRLETLLFTRQGDGF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 176 ------------------SANMLNEEVEWQQKSYDGVINGSFYVSARNAGIPANHIQKIANLFQWRLNFAKDLQRGDKFK 237
Cdd:COG3061 149 qrkrvtelsdgsfsadaaLASLETLELAAAAGILSDFIAAALDAGAGDAGLVELEIILDDDIDFADLLFAADRFTGDYFR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 238 VLVRQETVEGKSTGNTQLLGVEVFSQGKTVSAWLSEDGNYYDGQANSLERGFRRYPTHSRYRVSSNFNPARRHPITGQVR 317
Cdd:COG3061 229 VYAEGEGGDGGYIGAGGFRAAKFRRRAVRFRRSSSSSSYRRRPHRLSRRRRLRRGPDAAAPSGSSNAAGGGGHKITRRGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 318 PHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGNTGRSTGA 397
Cdd:COG3061 309 GGGGAAVGVGTGTPTTGAGLGVVRGGRGGGGGVVVGQIGRGGTYGGTGLHLHKHGHKGGGVVGQGVTIGTLGGTGPTTGP 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 759408745 398 HLHYEVRLNNRPVDAMKVKLPMAEPLSGKDKRQFLAK 434
Cdd:COG3061 389 HLHYEFVQNGVRVAPLTVKLPAAPPLAAAAAAAFKAL 425
|
|
| NlpD |
COG0739 |
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ... |
227-418 |
3.52e-57 |
|
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440502 [Multi-domain] Cd Length: 196 Bit Score: 187.10 E-value: 3.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 227 AKDLQRGDKFKVLVRQETVEGKSTGNTQLLGVEVFSQGKTVSAWLSEDGNYYDGQANSLERGFRRYPTHSRyrVSSNFNP 306
Cdd:COG0739 8 AAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGR--ITSGFGY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 307 aRRHPITGQVRPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIA 386
Cdd:COG0739 86 -RRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIG 164
|
170 180 190
....*....|....*....|....*....|..
gi 759408745 387 LSGNTGRSTGAHLHYEVRLNNRPVDAMKVKLP 418
Cdd:COG0739 165 YVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
|
|
| Peptidase_M23 |
pfam01551 |
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ... |
317-411 |
5.06e-44 |
|
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
Pssm-ID: 460250 [Multi-domain] Cd Length: 96 Bit Score: 149.23 E-value: 5.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 317 RPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGNTGRSTG 396
Cdd:pfam01551 1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80
|
90
....*....|....*
gi 759408745 397 AHLHYEVRLNNRPVD 411
Cdd:pfam01551 81 PHLHFEIRKNGKPVD 95
|
|
| Csd3_N2 |
pfam19425 |
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This ... |
183-306 |
6.85e-41 |
|
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This domain has a similar structure to pfam18059 despite low sequence similarity.
Pssm-ID: 437257 [Multi-domain] Cd Length: 122 Bit Score: 141.77 E-value: 6.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 183 EVEWQQKSYDGVINGSFYVSARNAGIPANHIQKIANLFQWRLNFAKdLQRGDKFKVLVRQETVEGKSTgNTQLLGVEVFS 262
Cdd:pfam19425 1 EGEWQNSVLKGRVDGSFVASARKAGLTSNEISAVIKALQWQLDFRK-LKKGDKFSVLMSREMLDGKRE-QSQLLGVRLRS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 759408745 263 QGKTVSAWLSEDGNYYDGQANSLERGFRRYPTHSRYRVSSNFNP 306
Cdd:pfam19425 79 GGKDYYAIRAEDGKFYDRNGSGLARGFLRFPTAKQFRVSSNFNP 122
|
|
| M23_peptidase |
cd12797 |
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ... |
319-403 |
6.87e-39 |
|
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 135.03 E-value: 6.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 319 HEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGNTGRSTGAH 398
Cdd:cd12797 1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80
|
....*
gi 759408745 399 LHYEV 403
Cdd:cd12797 81 LHFEI 85
|
|
| SpoIIQ2 |
COG5821 |
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ... |
310-415 |
3.21e-37 |
|
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444523 [Multi-domain] Cd Length: 200 Bit Score: 134.77 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 310 HPITGQVRPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHL-SKLLVKPGQKVKMGDKIALS 388
Cdd:COG5821 88 SKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANLdSKIKVKVGQKVKKGQVIGKV 167
|
90 100 110
....*....|....*....|....*....|
gi 759408745 389 GNTGR---STGAHLHYEVRLNNRPVDAMKV 415
Cdd:COG5821 168 GSTALfesSEGPHLHFEVLKNGKPVDPMKY 197
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-414 |
5.14e-26 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 108.70 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 299 RVSSNFNPARrhpitGQVRPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQK 378
Cdd:COG4942 262 RVVRRFGERD-----GGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQR 336
|
90 100 110
....*....|....*....|....*....|....*.
gi 759408745 379 VKMGDKIALSGNTGRSTGAHLHYEVRLNNRPVDAMK 414
Cdd:COG4942 337 VKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLP 372
|
|
| SpoIVFA |
COG5833 |
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ... |
311-415 |
6.34e-10 |
|
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444535 [Multi-domain] Cd Length: 219 Bit Score: 58.85 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 311 PITGQV-----RPHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKI 385
Cdd:COG5833 107 PVSGKVvesfqENGKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKI 186
|
90 100 110
....*....|....*....|....*....|..
gi 759408745 386 alsGNTGRSTG--AHLHYEVRLNNRPVDAMKV 415
Cdd:COG5833 187 ---GTVPATEGeeGTFYFAIKKGGKFIDPIQV 215
|
|
| nlpD |
PRK10871 |
murein hydrolase activator NlpD; |
320-414 |
1.01e-09 |
|
murein hydrolase activator NlpD;
Pssm-ID: 236782 [Multi-domain] Cd Length: 319 Bit Score: 59.46 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 320 EGTDFALPVGTPVMATGDGVVL---KATRHplAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGNTGRSTg 396
Cdd:PRK10871 220 KGIDIAGSKGQAIIATADGRVVyagNALRG--YGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS- 296
|
90
....*....|....*...
gi 759408745 397 AHLHYEVRLNNRPVDAMK 414
Cdd:PRK10871 297 TRLHFEIRYKGKSVNPLR 314
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
311-411 |
1.24e-07 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 53.54 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 311 PITGQVRpHEGTDFALPVGTPVMATGDGVVLKATRHPLAGTYVVIKHGRTLMTRYLHLSKLLVKPGQKVKMGDKIALSGN 390
Cdd:PRK11637 322 QLQGELR-WKGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGS 400
|
90 100
....*....|....*....|.
gi 759408745 391 TGRSTGAHLHYEVRLNNRPVD 411
Cdd:PRK11637 401 SGGQGRPSLYFEIRRQGQAVN 421
|
|
| OapA |
pfam04225 |
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the ... |
96-175 |
3.43e-07 |
|
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: 47.73 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 96 QWQDYRVRNGENLTTIFNNLGLSTTTLYKVLDAD-AKNNLARLKPGQTIELLIDQDNILQQLKIRLNIKQTLVLERTDDT 174
Cdd:pfam04225 1 NWKTYTVPKGDTLAQLFRDNNLPISDVNAMAKVEgADKPLSNIKSGQLVRIKLNAQGRVDELQIENGAKSVMFFRQSDGS 80
|
.
gi 759408745 175 Y 175
Cdd:pfam04225 81 F 81
|
|
| PRK06148 |
PRK06148 |
hypothetical protein; Provisional |
309-403 |
6.06e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 180426 [Multi-domain] Cd Length: 1013 Bit Score: 45.40 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759408745 309 RHPITGQVRPHEGTDFALPVGTPVMATGDGVVLKAT--RHPLA-GTYVVIKH----GRTLMTRYLHLSKLLV---KPGQK 378
Cdd:PRK06148 431 RFIEGERRTVHLGVDLFAPAGTPVYAPLAGTVRSVEieAVPLGyGGLVALEHetpgGDPFYTLYGHLAHEAVsrlKPGDR 510
|
90 100
....*....|....*....|....*..
gi 759408745 379 VKMGDKIALSGNTGRSTG--AHLHYEV 403
Cdd:PRK06148 511 LAAGELFGAMGDAHENGGwaPHLHFQL 537
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
91-145 |
2.70e-03 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 40.10 E-value: 2.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 759408745 91 ADGTPQWQ-DYRVRNGENLTTIFNNLGLSTTTLYKVldadakNNL--ARLKPGQTIEL 145
Cdd:PRK10783 336 ADNTPLNSrSYKVRSGDTLSGIASRLNVSTKDLQQW------NNLrgSKLKVGQTLTI 387
|
|
| |
