Species | Limosilactobacillus sp900557215 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus sp900557215 | |||||||||||
CAZyme ID | MGYG000002593_00976 | |||||||||||
CAZy Family | GH25 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 45497; End: 46711 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 36 | 211 | 1.5e-27 | 0.9887005649717514 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06415 | GH25_Cpl1-like | 2.10e-52 | 33 | 219 | 1 | 196 | Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage. |
smart00641 | Glyco_25 | 9.33e-17 | 118 | 225 | 2 | 109 | Glycosyl hydrolases family 25. |
pfam01183 | Glyco_hydro_25 | 3.07e-16 | 36 | 212 | 1 | 180 | Glycosyl hydrolases family 25. |
cd00118 | LysM | 1.16e-11 | 254 | 296 | 3 | 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. |
smart00257 | LysM | 4.01e-11 | 254 | 296 | 2 | 44 | Lysin motif. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QAR22460.1 | 1.03e-196 | 29 | 404 | 42 | 413 |
QFG73426.1 | 1.58e-175 | 29 | 404 | 21 | 396 |
QIZ05292.1 | 6.19e-174 | 29 | 404 | 14 | 392 |
QDK49467.1 | 2.73e-164 | 11 | 404 | 5 | 397 |
QLL70978.1 | 1.11e-151 | 14 | 404 | 1 | 408 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6AKV_A | 7.26e-09 | 331 | 404 | 205 | 282 | ChainA, LysB4 [Bacillus phage B4] |
5A6S_A | 6.19e-07 | 20 | 227 | 1 | 207 | Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8HA43 | 2.50e-14 | 98 | 218 | 210 | 342 | D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2 |
P39046 | 2.13e-06 | 254 | 299 | 338 | 382 | Muramidase-2 OS=Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) OX=768486 GN=EHR_05900 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000260 | 0.998939 | 0.000270 | 0.000200 | 0.000174 | 0.000154 |
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