hypothetical protein NMCA_24860 [Enterobacter ludwigii]
PRK15396 family protein( domain architecture ID 10015102)
PRK15396 family protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||
PRK15396 | PRK15396 | major outer membrane lipoprotein; |
1-78 | 9.11e-40 | ||
major outer membrane lipoprotein; : Pssm-ID: 185294 Cd Length: 78 Bit Score: 125.77 E-value: 9.11e-40
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Name | Accession | Description | Interval | E-value | |||
PRK15396 | PRK15396 | major outer membrane lipoprotein; |
1-78 | 9.11e-40 | |||
major outer membrane lipoprotein; Pssm-ID: 185294 Cd Length: 78 Bit Score: 125.77 E-value: 9.11e-40
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Lpp | COG4238 | Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis]; |
1-78 | 6.04e-32 | |||
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443380 [Multi-domain] Cd Length: 77 Bit Score: 105.82 E-value: 6.04e-32
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LPP | pfam04728 | Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer ... |
26-78 | 3.43e-18 | |||
Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes. Pssm-ID: 428092 [Multi-domain] Cd Length: 53 Bit Score: 70.46 E-value: 3.43e-18
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Ala_zip_lipo | NF040598 | Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
4-75 | 8.21e-13 | |||
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope. Pssm-ID: 468572 [Multi-domain] Cd Length: 90 Bit Score: 57.69 E-value: 8.21e-13
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Name | Accession | Description | Interval | E-value | |||
PRK15396 | PRK15396 | major outer membrane lipoprotein; |
1-78 | 9.11e-40 | |||
major outer membrane lipoprotein; Pssm-ID: 185294 Cd Length: 78 Bit Score: 125.77 E-value: 9.11e-40
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Lpp | COG4238 | Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis]; |
1-78 | 6.04e-32 | |||
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443380 [Multi-domain] Cd Length: 77 Bit Score: 105.82 E-value: 6.04e-32
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PRK09973 | PRK09973 | lipoprotein YqhH; |
3-72 | 3.19e-20 | |||
lipoprotein YqhH; Pssm-ID: 170188 Cd Length: 85 Bit Score: 76.57 E-value: 3.19e-20
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LPP | pfam04728 | Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer ... |
26-78 | 3.43e-18 | |||
Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes. Pssm-ID: 428092 [Multi-domain] Cd Length: 53 Bit Score: 70.46 E-value: 3.43e-18
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Ala_zip_lipo | NF040598 | Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
4-75 | 8.21e-13 | |||
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope. Pssm-ID: 468572 [Multi-domain] Cd Length: 90 Bit Score: 57.69 E-value: 8.21e-13
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Blast search parameters | ||||
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