MULTISPECIES: phosphonate ABC transporter, permease protein PhnE [Rhizobium]
PhnE/PtxC family ABC transporter permease( domain architecture ID 11466536)
PhnE/PtxC family ABC transporter permease is the transmembrane subunit found in a periplasmic binding protein (PBP)-dependent ABC transport system, which may be involved in the transport of phosphonate, phosphate, or phosphite ions
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
PhnE | COG3639 | ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport ... |
216-442 | 2.11e-73 | ||||
ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport and metabolism]; : Pssm-ID: 442856 [Multi-domain] Cd Length: 244 Bit Score: 230.74 E-value: 2.11e-73
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Name | Accession | Description | Interval | E-value | ||||
PhnE | COG3639 | ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport ... |
216-442 | 2.11e-73 | ||||
ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport and metabolism]; Pssm-ID: 442856 [Multi-domain] Cd Length: 244 Bit Score: 230.74 E-value: 2.11e-73
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PhnE | TIGR01097 | phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound ... |
246-441 | 2.87e-63 | ||||
phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound analogous to organic phosphates, but in which the C-O-P linkage is replaced by a direct, stable C-P bond. Some bacteria can utilize phosphonates as a source of phosphorus. This family consists of permease proteins of known or predicted phosphonate ABC transporters. Often this protein is found as a duplicated pair, occasionally as a fused pair. Certain "second" copies score in between the trusted and noise cutoff and should be considered true hits (by context). [Transport and binding proteins, Anions] Pssm-ID: 273441 [Multi-domain] Cd Length: 250 Bit Score: 204.70 E-value: 2.87e-63
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TM_PBP2 | cd06261 | Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ... |
250-432 | 1.66e-09 | ||||
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others. Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 57.29 E-value: 1.66e-09
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Name | Accession | Description | Interval | E-value | ||||
PhnE | COG3639 | ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport ... |
216-442 | 2.11e-73 | ||||
ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport and metabolism]; Pssm-ID: 442856 [Multi-domain] Cd Length: 244 Bit Score: 230.74 E-value: 2.11e-73
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PhnE | TIGR01097 | phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound ... |
246-441 | 2.87e-63 | ||||
phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound analogous to organic phosphates, but in which the C-O-P linkage is replaced by a direct, stable C-P bond. Some bacteria can utilize phosphonates as a source of phosphorus. This family consists of permease proteins of known or predicted phosphonate ABC transporters. Often this protein is found as a duplicated pair, occasionally as a fused pair. Certain "second" copies score in between the trusted and noise cutoff and should be considered true hits (by context). [Transport and binding proteins, Anions] Pssm-ID: 273441 [Multi-domain] Cd Length: 250 Bit Score: 204.70 E-value: 2.87e-63
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TM_PBP2 | cd06261 | Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ... |
250-432 | 1.66e-09 | ||||
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others. Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 57.29 E-value: 1.66e-09
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Blast search parameters | ||||
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