hypothetical protein [Alistipes shahii]
OmpA family protein( domain architecture ID 1000806)
OmpA family membrane protein acts as a porin with low permeability that allows slow penetration of small solutes, similar to peptidoglycan-associated lipoprotein that is involved in maintenance of the integrity of the cell cell envelope
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
NlpI super family | cl34822 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
387-540 | 1.08e-05 | ||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; The actual alignment was detected with superfamily member COG4785: Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 46.83 E-value: 1.08e-05
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OmpA_C-like super family | cl30079 | Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ... |
292-368 | 8.70e-04 | ||||
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane. The actual alignment was detected with superfamily member cd07185: Pssm-ID: 453091 [Multi-domain] Cd Length: 106 Bit Score: 39.07 E-value: 8.70e-04
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Name | Accession | Description | Interval | E-value | ||||
NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
387-540 | 1.08e-05 | ||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 46.83 E-value: 1.08e-05
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OmpA_C-like | cd07185 | Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ... |
292-368 | 8.70e-04 | ||||
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane. Pssm-ID: 143586 [Multi-domain] Cd Length: 106 Bit Score: 39.07 E-value: 8.70e-04
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Name | Accession | Description | Interval | E-value | ||||
NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
387-540 | 1.08e-05 | ||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 46.83 E-value: 1.08e-05
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OmpA_C-like | cd07185 | Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ... |
292-368 | 8.70e-04 | ||||
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane. Pssm-ID: 143586 [Multi-domain] Cd Length: 106 Bit Score: 39.07 E-value: 8.70e-04
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Blast search parameters | ||||
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