Species | Citrobacter_B koseri | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_B; Citrobacter_B koseri | |||||||||||
CAZyme ID | MGYG000002494_04543 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | putative protein YgaU | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4553853; End: 4554302 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK11198 | PRK11198 | 7.00e-84 | 1 | 148 | 1 | 147 | LysM domain/BON superfamily protein; Provisional |
COG1652 | XkdP | 6.36e-21 | 1 | 149 | 53 | 264 | Nucleoid-associated protein YgaU, contains BON and LysM domains [Function unknown]. |
pfam04972 | BON | 1.52e-11 | 23 | 88 | 1 | 66 | BON domain. This domain is found in a family of osmotic shock protection proteins. It is also found in some Secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. |
cd00118 | LysM | 4.07e-11 | 97 | 146 | 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. |
smart00257 | LysM | 3.95e-10 | 98 | 146 | 1 | 44 | Lysin motif. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASE83475.1 | 2.64e-103 | 1 | 149 | 1 | 149 |
AVE69930.1 | 2.64e-103 | 1 | 149 | 1 | 149 |
AYY74370.1 | 2.64e-103 | 1 | 149 | 1 | 149 |
ATF98673.1 | 2.64e-103 | 1 | 149 | 1 | 149 |
AVE58576.1 | 2.64e-103 | 1 | 149 | 1 | 149 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5FIM_A | 1.87e-97 | 1 | 149 | 1 | 149 | Thestructure of Kbp.K from E. coli [Escherichia coli],7PVC_A Chain A, Potassium binding protein Kbp [Escherichia coli K-12] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0ADE6 | 7.79e-97 | 1 | 149 | 1 | 149 | Potassium binding protein Kbp OS=Escherichia coli (strain K12) OX=83333 GN=kbp PE=1 SV=2 |
P0ADE7 | 7.79e-97 | 1 | 149 | 1 | 149 | Potassium binding protein Kbp OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=kbp PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000002 | 0.000035 | 0.000002 | 0.000000 | 0.000000 | 0.000000 |
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