Species | ||||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; | |||||||||||
CAZyme ID | MGYG000004840_00049 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 53119; End: 54159 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00877 | NLPC_P60 | 2.99e-29 | 244 | 340 | 1 | 100 | NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins. |
COG0791 | Spr | 6.81e-21 | 181 | 340 | 24 | 193 | Cell wall-associated hydrolase, NlpC family [Cell wall/membrane/envelope biogenesis]. |
PRK13914 | PRK13914 | 4.50e-12 | 9 | 325 | 200 | 460 | invasion associated endopeptidase. |
NF033742 | NlpC_p60_RipB | 4.49e-11 | 239 | 321 | 84 | 179 | NlpC/P60 family peptidoglycan endopeptidase RipB. |
cd00118 | LysM | 6.90e-11 | 9 | 53 | 1 | 45 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QFV01657.1 | 1.08e-107 | 1 | 346 | 18 | 349 |
AGR64855.1 | 1.02e-73 | 1 | 345 | 17 | 343 |
AXX74464.1 | 1.02e-73 | 1 | 345 | 17 | 343 |
AWD63352.1 | 1.91e-73 | 1 | 345 | 17 | 341 |
QQR13953.1 | 2.79e-73 | 1 | 345 | 17 | 342 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6B8C_A | 1.52e-27 | 236 | 344 | 32 | 142 | Crystalstructure of NlpC/p60 domain of peptidoglycan hydrolase SagA [Enterococcus faecium] |
6BIQ_A | 9.49e-09 | 240 | 336 | 163 | 265 | Structureof NlpC2 from Trichomonas vaginalis [Trichomonas vaginalis],6BIQ_B Structure of NlpC2 from Trichomonas vaginalis [Trichomonas vaginalis],6BIQ_C Structure of NlpC2 from Trichomonas vaginalis [Trichomonas vaginalis],6BIQ_D Structure of NlpC2 from Trichomonas vaginalis [Trichomonas vaginalis] |
2XIV_A | 1.19e-08 | 236 | 329 | 84 | 190 | Structureof Rv1477, hypothetical invasion protein of Mycobacterium tuberculosis [Mycobacterium tuberculosis H37Rv] |
3NE0_A | 1.26e-08 | 236 | 329 | 89 | 195 | Structureand functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation [Mycobacterium tuberculosis H37Rv] |
3PBC_A | 1.26e-08 | 236 | 329 | 89 | 195 | ChainA, Invasion Protein [Mycobacterium tuberculosis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P13692 | 4.77e-25 | 236 | 344 | 406 | 516 | Protein P54 OS=Enterococcus faecium OX=1352 PE=3 SV=2 |
P54421 | 1.92e-11 | 236 | 340 | 224 | 328 | Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1 |
O07532 | 1.01e-10 | 236 | 340 | 377 | 481 | Peptidoglycan endopeptidase LytF OS=Bacillus subtilis (strain 168) OX=224308 GN=lytF PE=1 SV=2 |
O31852 | 2.07e-10 | 236 | 340 | 303 | 407 | D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlS PE=1 SV=1 |
P76190 | 6.20e-09 | 243 | 329 | 152 | 245 | Murein DD-endopeptidase MepH OS=Escherichia coli (strain K12) OX=83333 GN=mepH PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.990847 | 0.009056 | 0.000057 | 0.000034 | 0.000015 | 0.000036 |
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