Species | Limosilactobacillus reuteri_E | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus reuteri_E | |||||||||||
CAZyme ID | MGYG000001336_01931 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1904225; End: 1905736 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00877 | NLPC_P60 | 2.36e-26 | 400 | 496 | 2 | 94 | NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins. |
cd00118 | LysM | 1.26e-17 | 103 | 146 | 2 | 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. |
NF033742 | NlpC_p60_RipB | 9.83e-17 | 400 | 492 | 90 | 190 | NlpC/P60 family peptidoglycan endopeptidase RipB. |
pfam01476 | LysM | 1.05e-16 | 104 | 147 | 1 | 43 | 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. |
PRK13914 | PRK13914 | 1.37e-16 | 11 | 482 | 2 | 460 | invasion associated endopeptidase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AEI58077.1 | 7.47e-289 | 1 | 503 | 1 | 503 |
QLL75721.1 | 4.77e-285 | 1 | 503 | 1 | 503 |
QLQ62351.1 | 1.94e-284 | 1 | 503 | 1 | 503 |
QIZ04030.1 | 2.75e-284 | 1 | 503 | 1 | 503 |
QDK48906.1 | 4.70e-227 | 1 | 503 | 1 | 477 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6B8C_A | 2.07e-23 | 401 | 499 | 42 | 139 | Crystalstructure of NlpC/p60 domain of peptidoglycan hydrolase SagA [Enterococcus faecium] |
2XIV_A | 3.26e-12 | 400 | 485 | 93 | 189 | Structureof Rv1477, hypothetical invasion protein of Mycobacterium tuberculosis [Mycobacterium tuberculosis H37Rv] |
3NE0_A | 3.54e-12 | 400 | 485 | 98 | 194 | Structureand functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation [Mycobacterium tuberculosis H37Rv] |
3PBC_A | 3.54e-12 | 400 | 485 | 98 | 194 | ChainA, Invasion Protein [Mycobacterium tuberculosis] |
4Q4T_A | 6.29e-12 | 400 | 485 | 356 | 452 | Structureof the Resuscitation Promoting Factor Interacting protein RipA mutated at E444 [Mycobacterium tuberculosis H37Rv] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P13692 | 8.09e-21 | 401 | 499 | 416 | 513 | Protein P54 OS=Enterococcus faecium OX=1352 PE=3 SV=2 |
O34669 | 7.72e-17 | 21 | 156 | 10 | 129 | Cell wall-binding protein YocH OS=Bacillus subtilis (strain 168) OX=224308 GN=yocH PE=1 SV=1 |
Q49UX4 | 6.90e-13 | 17 | 156 | 5 | 139 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1 |
P9WHU4 | 7.24e-11 | 400 | 492 | 125 | 225 | Peptidoglycan endopeptidase RipB OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=ripB PE=3 SV=1 |
P9WHU5 | 7.24e-11 | 400 | 492 | 125 | 225 | Peptidoglycan endopeptidase RipB OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=ripB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000473 | 0.998700 | 0.000198 | 0.000244 | 0.000182 | 0.000157 |
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