BioAssay record AID 676749 submitted by ChEMBL: Inhibition of Multidrug resistance efflux pump in Mycobacterium smegmatis str. MC2 155 ATCC 700084 assessed as reduction in isoniazid bromide MIC presence of test compound at 64 mg/L.
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Multidrug efflux systems display the ability to transport a variety of structurally unrelated drugs from a cell and consequently are capable of conferring resistance to a diverse range of chemotherapeutic agents. This review examines multidrug efflux systems which use the proton motive force to drive drug transport. These proteins are likely to operate as multidrug/proton antiporters and have been identified in both prokaryotes and eukaryotes. Such proton-dependent multidrug efflux proteins belong to three distinct families or superfamilies of transport proteins: the major facilitator superfamily (MFS), the small multidrug resistance (SMR) family, and the resistance/ nodulation/cell division (RND) family. The MFS consists of symporters, antiporters, and uniporters with either 12 or 14 transmembrane-spanning segments (TMS), and we show that within the MFS, three separate families include various multidrug/proton antiport proteins. The SMR family consists of proteins with four TMS, and the ...
The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role ...
Recent identification of several members of the chloroplastic protein translocation machinery has allowed for further refinement of our understanding of the mechanism by which precursors are transported into chloroplasts. We have attempted to define the composition of complexes that form during translocation using co‐immunoprecipitation techniques with antibodies specific to translocation components. We have observed that precursors could be found in stable association with translocation complexes after solubilization with a mild detergent, decylmaltoside. Characterization of these complexes has led to two conclusions: (i) that under limiting ATP conditions, precursors associated with translocation complexes containing components of the outer and inner envelope membranes; and (ii) that the chaperone ClpC, a stromal Hsp100 homolog, was associated with precursor‐containing complexes under these limiting ATP conditions.. The data presented here suggest a new role for the stromal Hsp100 homolog ...
Membrane transporters allow the selective transport of otherwise poorly permeable solutes across the cell membrane and thus, play a key role in maintaining cellular homeostasis in all kingdoms of life. Importantly, these proteins also serve as important drug targets. Over the last decades, major progress in structural biology methods has elucidated important structure-function relationships in mem...
Proteoliposomes represent a suitable and up to date tool for studying membrane transporters which physiologically mediate absorption, excretion, trafficking and reabsorption of nutrients and metabolites. Using recently developed reconstitution strategies, transporters can be inserted in artificial bilayers with the same orientation as in the cell membranes and in the absence of other interfering molecular systems. These methodologies are very suitable for studying kinetic parameters and molecular mechanisms. After the first applications on mitochondrial transporters, in the last decade, proteoliposomes obtained with optimized methodologies have been used for studying plasma membrane transporters and defining their functional and kinetic properties and structure/function relationships. A lot of information has been obtained which has clarified and completed the knowledge on several transporters among which the OCTN sub-family members, transporters for neutral amino acid, B0AT1 and ASCT2, and others.
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Johnson, Tanya and Ouhtit, Allal and Gaur, Rajiv and Fernando, Augusta and Schwarzenberger, Paul and Su, Joseph and Ismail, Mohamed F and El-Sayyad, Hassan I and Karande, Anjali and Elmageed, Zakaria Abd and Rao, Prakash and Raj, Madhwa (2009) Biochemical characterization of riboflavin carrier protein (RCP) in prostate cancer. In: Frontiers in Bioscience, 14 . pp. 3634-3640. ...
Raj, Madhwa HG and Roy, Tanya and Karande, Anjali and Rao, Prakash N and Richardson, Kevin and Raj, Shailaja G (2003) Expression patterns of Riboflavin Carrier Protein (RCP) in the female reproductive system. In: Fertility and Sterility, 80 (3). S249-S250. ...
Plant nutrition critically depends on the activity of membrane transporters that translocate minerals from the soil into the plant and are responsible for their intra- and intercellular distribution. Most plant membrane transporters are encoded by multigene families whose members often exhibit overlapping expression patterns and a high degree of sequence homology. Furthermore, many inorganic nutrients are transported by more than one transporter family. These considerations, coupled with a large number of so-far non-annotated putative transporter genes, hamper our progress in understanding how the activity of specific transporters is integrated into a response to fluctuating conditions. We designed an oligonucleotide microarray representing 1096 Arabidopsis transporter genes and analysed the root transporter transcriptome over a 96-h period with respect to 80 mm NaCl, K+ starvation and Ca2+ starvation. Our data show that cation stress led to changes in transcript level of many genes across most ...
CP000667.PE394 Location/Qualifiers FT CDS_pept 453881..454846 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Strop_0394" FT /product="RarD protein, DMT superfamily transporter" FT /note="TIGRFAM: RarD protein, DMT superfamily transporter; FT PFAM: protein of unknown function DUF6, transmembrane" FT /db_xref="EnsemblGenomes-Gn:Strop_0394" FT /db_xref="EnsemblGenomes-Tr:ABP52879" FT /db_xref="GOA:A4X1X9" FT /db_xref="InterPro:IPR000620" FT /db_xref="InterPro:IPR004626" FT /db_xref="UniProtKB/TrEMBL:A4X1X9" FT /protein_id="ABP52879.1" FT /translation="MTPRKLGYLYGIGAYVLWGFFPLYMRLLRPASPLEILAHRIVWSV FT VFVALVLAAMRNRSFLRALLRRPRALAALGIAAALVALNWGTYIYGVNSERVVETSLGY FT FVNPLVVVLLGVFVLRERLRPAQWAAIGVGGAAVVVLTVDYGRPPYLALVLSFTFAGYG FT LVKKRLGLPAAQGLFVESAVLALPALAYLAWLGGTGGATFGAVSAGHTALLISAGAATA FT IPLLMFAGAANRLPFTSLGMLQYLAPILQLGCGVIIFREPMPPARLAGFALVWLALAVF FT TVDAVRAARRLPPPLADEVLAAVQPGSGTSPQQERKIVSG" gtgacgcctc gcaagctcgg ctacctgtac ggtatcggcg cgtacgtgct ctggggtttc 60 ttcccgctct acatgagact gctccggccg ...
Membrane protein topology predictions can be markedly improved by the inclusion of even very limited experimental information. We have recently introduced an approach for the production of reliable topology models based on a combination of experimental determination of the location (cytoplasmic or p …
CP000386.PE141 Location/Qualifiers FT CDS complement(147289..148863) FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Rxyl_0143" FT /product="SSS sodium solute transporter superfamily" FT /note="TIGRFAM: SSS sodium solute transporter superfamily; FT PFAM: Na+/solute symporter; KEGG: gka:GK0928 sodium:solute FT symporter" FT /db_xref="EnsemblGenomes-Gn:Rxyl_0143" FT /db_xref="EnsemblGenomes-Tr:ABG03122" FT /db_xref="GOA:Q1AZQ6" FT /db_xref="InterPro:IPR001734" FT /db_xref="InterPro:IPR038377" FT /db_xref="UniProtKB/TrEMBL:Q1AZQ6" FT /protein_id="ABG03122.1" FT /translation="MSDRAIATIFFVLIIVLTLGITAWAARRNKDTAHHYVAGGEIKGW FT QNGLAISGDYLSAASFLGIAGSIALTGFSGFYLSIGFLVAYLVVLLLVAEPLRNLGKYT FT FADMLAARFNLRSVRSAAALSTIAISTFYMIAQMVGAGALIELLLGLPYVASVVIIGVL FT MTIYIAAGGMVATTWIQIVKAVLLISGTLALSIAVLAQFGFNPVAIFDRVEAELGPEMV FT LPPPPEGFVSGIDVVSLNIALVFGTAGLPHILMRFLTVPDAKTARNSIIVATWIIGLFY FT LMTPIMGYGAALLVGQDVIAEQNPAGNTAAPQLAGELGGPIFLAFISAVAFATIVAVVA FT GLVIAASSAFAHDFYTNVIRGGEASEQEQFRAARIAAVAVSLGAMFLAIFARDFNVSFL FT ...
This paper is interesting because it reports a novel method for the regulation of an ATPase required to drive polypeptides through the bacterial inner membrane via the transmembrane protein-conducting channel SecYEG. Protein translocation through the SecY / Sec61 complex is an essential and conserved reaction and in bacteria it proceeds by the action of an ATP-driven protein pump associated with the protein conduction channel. The work identifies a conserved salt bridge or gate in SecA that may form a switch to control different conformations in the nucleotide binding fold. As such, it may play an important role in relaying the conformational changes associated with ATP binding and hydrolysis to a power stroke responsible for the directional movement of polypeptides. ...
Genetic information processingProtein fateProtein and peptide secretion and traffickingTat (twin-arginine translocation) pathway signal sequence (TIGR01409; HMM-score: 25.5) ...
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TY - JOUR. T1 - Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB. AU - Luke,Iris. AU - Handford,Jennifer I.. AU - Palmer,Tracy. AU - Sargent,Frank. PY - 2009/12. Y1 - 2009/12. N2 - The twin-arginine translocation (Tat) apparatus is a protein targeting system found in the cytoplasmic membranes of many prokaryotes. Substrate proteins of the Tat pathway are synthesised with signal peptides bearing SRRxFLK twin-arginine amino acid motifs. All Tat signal peptides have a common tripartite structure comprising a polar N-terminal region, followed by a hydrophobic region of variable length and a polar C-terminal region. In Escherichia coli, Tat signal peptides are proteolytically cleaved after translocation. The signal peptide C-terminal regions contain conserved AxA motifs, which are possible recognition sequences for leader peptidase I (LepB). In this work, the role of LepB in Tat signal peptide processing was addressed directly. Deliberate repression of lepB ...
The Tat system is a protein export system dedicated to the transport of folded proteins across the prokaryotic cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. Proteins are targeted for export by the Tat system via N-terminal signal peptides harbouring an S-R-R-x-F-L-K twin-arginine motif. In this chapter qualitative and quantitative assays for native Tat substrates in the model organism Escherichia coli are described. Genetic screening methods designed to allow the rapid positive selection of Tat signal peptide activity and the first positive selection for mutations that inactivate the Tat pathway are also presented. Finally isothermal titration calorimetry (ITC) methods for measuring the affinity of twin-arginine signal peptide-chaperone interactions are discussed.
Escherichia coli K1 infection is a major cause of neonatal meningitis, with high rates of mortality and disability. Despite years of research, only a small number of factors contributing to E. coli K1 virulence have been identified. The Tat (twin-arginine translocation) protein export system is found in the cytoplasmic membrane of E. coli and is involved in the transport of folded proteins. In vivo and ex vivo models using the African migratory locust, Locusta migratoria, were employed to explore the role of Tat pathway in E. coli K1 virulence using tat-deletion mutants. Groups of locusts were infected and mortality was recorded at 24-h intervals. The findings revealed that ?tatA, Delta tatAC and ?tat produced levels of mortality similar to wild-type E. coli K1, with |78% mortality recorded within 72 h. Bacteraemia was determined from haemolymph obtained 3 and 24 h postinfection. Again, wild-type and ?tatA produced similar levels of bacteraemia. In contrast, Delta tatAC and ?tat produced lower levels of
Hgt1p, a high-affinity glutathione transporter from Saccharomyces cerevisiae belongs to the recently described family of OPTs (oligopeptide transporters), the majority of whose members still have unknown substrate specificity. To obtain insights into substrate recognition and translocation, we have subjected all 21 residues of TMD9 (transmembrane domain 9) to alanine-scanning mutagenesis. Phe523 was found to be critical for glutathione recognition, since F523A mutants showed a 4-fold increase in Km without affecting expression or localization. Phe523 and the previously identified polar residue Gln526 were on the same face of the helix suggesting a joint participation in glutathione recognition, whereas two other polar residues, Ser519 and Asn522, of TMD9, although also orientated on the same face, did not appear to be involved. The size and hydrophobicity of Phe523 were both key features of its functionality, as seen from mutational analysis. Sequence alignments revealed that Phe523 and Gln526 ...
A major feature of the MexAB-OprM multidrug efflux pump which distinguishes it from the MexCD-OprJ and MexEF-OprN multidrug efflux systems in Pseudomonas aeruginosa is its ability to export a wide variety of beta-lactam antibiotics. Given the periplasmic location of their targets it is feasible that beta-lactams exit the cell via the outer membrane OprM without interaction with MexA and MexB, though the latter appear to be necessary for OprM function. To test this, chimeric MexAB-OprJ and MexCD-OprM efflux pumps were reconstituted in delta mexCD delta oprM and delta mexAB delta oprJ strains, respectively, and the influence of the exchange of outer membrane components on substrate (i.e., beta-lactam) specificity was assessed. Both chimeric pumps were active in antibiotic efflux, as evidenced by their contributions to resistance to a variety of antimicrobial agents, although there was no change in resistance profiles relative to the native pumps, indicating that OprM is not the determining factor ...
Bacteria have mechanisms to export proteins for diverse purposes, including colonization of hosts and pathogenesis. A small number of archetypal bacterial secretion machines have been found in several groups of bacteria and mediate a fundamentally distinct secretion process. Perhaps erroneously, proteins called autotransporters have long been thought to be one of these protein secretion systems. Mounting evidence suggests that autotransporters might be substrates to be secreted, not an autonomous transporter system. We have discovered a new translocation and assembly module (TAM) that promotes efficient secretion of autotransporters in proteobacteria. Functional analysis of the TAM in Citrobacter rodentium, Salmonella enterica and Escherichia coli showed that it consists of an Omp85-family protein, TamA, in the outer membrane and TamB in the inner membrane of diverse bacterial species. The discovery of the TAM provides a new target for the development of therapies to inhibit colonization by ...
Calcium- and potassium-permeable plasma membrane transporters are activated by copper in |i|Arabidopsis|/i| root tips: linking copper transport with cytosolic hydroxyl radical production
P. aeruginosa is known for its ability to develop resistance to a number of structurally unrelated antibiotics, a phenomenon which can now be attributed predominantly to chromosomal mutations leading to overexpression of multidrug efflux systems.P. aeruginosa also produces a series of exoproducts, several of which, such as elastase, alkaline protease, exotoxins, and pyocyanin, have been shown to be virulence factors (3, 54,55). In this study, we show a link between the active efflux system MexEF-OprN and the production of virulence factors regulated by the las (10, 11, 19) and rhl(2, 33) cell-to-cell signaling systems. This important finding suggests that P. aeruginosa strains becoming resistant to multiple antibiotics by overexpression of MexEF-OprN are likely to be less virulent. Indeed, we recently found that nfxC mutants exhibit significantly reduced virulence both in a nonmammalian system and in a rat model of acute pneumonia (P. Cosson et al., submitted for publication).. The connection ...
YidC is a polytopic inner membrane protein with a molecular mass of 60 kDa. To facilitate its purification, a histidine tag was introduced at the C‐terminus of YidC, and the gene was placed under control of the lac promoter yielding the expression vector pEH1hisYidC. To determine whether His‐tagged YidC is functional in vivo, pEH1hisYidC was transformed to the YidC depletion strain JS7131 (Samuelson et al., 2000). In this strain, the chromosomal yidC gene is disrupted and an intact yidC gene under control of the araBAD promoter has been introduced. JS7131 is not viable on Luria-Bertani (LB) agar plates containing 0.2% glucose, since under these conditions expression of yidC from the araBAD promoter is tightly repressed. Transformation with pEH1hisYidC restored growth of JS7131 in the presence of glucose (Figure 1A), indicating that plasmid‐encoded, His‐tagged YidC is functional. For overproduction, pEH1hisYidC was transformed to strain E. coli SF100 (Baneyx and Georgiou, 1990). YidC ...
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Bacterial proteins with MCE domains were first described as being important for Mammalian Cell Entry. More recent evidence suggests they are components of lipid ABC transporters. In Escherichia coli, the single-domain protein MlaD is known to be part of an inner membrane transporter that is important for maintenance of outer membrane lipid asymmetry. Here we describe two multi MCE domain-containing proteins in Escherichia coli, PqiB and YebT, the latter of which is an orthologue of MAM-7 that was previously reported to be an outer membrane protein. We show that all three MCE domain-containing proteins localise to the inner membrane. Bioinformatic analyses revealed that MCE domains are widely distributed across bacterial phyla but multi MCE domain-containing proteins evolved in Proteobacteria from single-domain proteins. Mutants defective in mlaD, pqiAB and yebST were shown to have distinct but partially overlapping phenotypes, but the primary functions of PqiB and YebT differ from MlaD. Complementing
The translocase of the outer membrane (TOM complex) forms the entry gate for the majority of mitochondrial precursor proteins. Subsequently, specific protein complexes sort the precurcor proteins into the different subcompartments. The presequence translocase (TIM23 complex) transport proteins across and into the inner membrane. The TIM23 complex cooperates with the presequence-translocase associated motor (PAM) for transport into the mitochondrial matrix. The carrier translocase (TIM22 complex) inserts proteins into the inner membrane. The activity of the respiratory chain generates a membrane potential that drives both protein import pathways. The MIA machinery transports cysteine-rich proteins into the intermembrane space. Outer membrane proteins with β-barrel structure are first transported across the TOM machinery and then inserted into the outer membrane by the sorting and assembly machinery (SAM complex). Finally, the mitochondrial import machinery (MIM) promotes biogenesis of outer ...
Outer membrane (OM) proteins 5, 6, 7, 20, 22, 37, 40, and 70 are subunits of the TOM system that transports proteins across the outer membrane. Proteins 9, 10, 12, 22 and 54 are subunits of the TIM system that mediates import of multispanning carrier proteins into the inner membrane (IM). A carrier precursor exiting the TOM channel is captured by the 70 kDa Tim9/10-complex in the intermembrane space and transferred to the 300 kDa inner membrane complex that contains Tim9p, Tim10p, Tim12p, Tim22p and Tim54p. Binding to the Tim22-complex triggers the membrane potential dependent insertion of mulitspanning carrier into the inner membrane. Inner membrane proteins 11, 17, 23 and 44 are members of, or closely adjacent to, the second TIM system (Tim17-complex)that mediates transport of precursors carrying a targeting presequence ...
Atypical SLCs are novel plausible secondary active or facilitative transansporter proteins that share ancestral background with the known solute carriers. However, they have not been assigned a name according to the SLC root system, or been classified into any of the existing SLC families. Most ataypical SLCs are families within the major facilitator superfamily (MFS). These atypical SLCs are plausible secondary active or facilitative transporter proteins that share ancestry with the known solute carriers. They are, however, not named according to the SLC root system, or classified into any of the existing SLC families. ATMFs are categorised based on their sequence similarity and phylogenetic closeness. Some Atypical SLC of MFS type are: OCA2, CLN3, SPNS1, SPNS2, SPNS3, SV2A, SV2B, SV2C, SVOP, SVOPL, MFSD1, MFSD2A, MFSD2B, MFSD3, MFSD4A, MFSD4B, MFSD5, MFSD6, MFSD6L, MFSD8, MFSD9, MFSD10, MFSD11, MFSD12, MFSD13A, MFSD14A, MFSD14B, UNC93A and UNC93B1. All these are ataypical SLCs found within the ...
Amino acid permeases are integral membrane proteins involved in the transport of amino acids into the cell. A number of such proteins have been found to be evolutionary related [(PUBMED:3146645)], [(PUBMED:2687114)], [(PUBMED:8382989)]. These proteins seem to contain up to 12 transmembrane segments. The best conserved region in this family is located in the second transmembrane segment.. This domain is found in amino acid permeases, as well as in solute carrier family 12A (SLC12A) members.. ...
Figure 4. The mature domain-binding site onto SecA. (A) The E. coli SecA (gray)-SeYEG (yellow) was modeled after the Thermotoga maritima translocase in three conformational states, based on PBD (purple) positioning: closed (left), open (middle), and wide open (right). Side and bottom views are shown (as indicated). I, II: SecA clamps. (B) Kd measurements of PhoA and its signal peptide (SPPhoA) for the wild-type (WT), locked closed (LC), locked open (LO), and locked wide open (LWO) SecA bound to SecYEG-inverted membrane vesicles. proPhoA(1-30) was used as SPPhoA. Affinity values represent means ± SEM; n = 3. (C) Potential space occupied by an incoming preprotein onto the cytoplasmic side (platform) of a SecA(gray)-SecYEG(yellow) translocase; signal peptide is in green. The inner circle represents the minimum area a translocation-competent preprotein would occupy, depicted here by the predicted DH of the smallest known preprotein (proEcnA; ∼3 nm; Table S8). The bigger circle represents the area ...
Remy, Estelle, et al. "A Major Facilitator Superfamily Transporter Plays a Dual Role in Polar Auxin Transport and Drought Stress Tolerance in Arabidopsis." Plant Cell, vol. 25, no. 3, American Society of Plant Biologists, 2013, pp. 901-26, doi:10.1105/tpc.113.110353 ...
Approximately 20% of bacterial proteins have functions outside the cytoplasm ( 1 ). Consequently, all bacteria possess protein export pathways that transport proteins made in the cytoplasm beyond the cytoplasmic membrane. These exported proteins may remain in the bacterial cell envelope or be further secreted to the extracellular environment. Many exported proteins function in essential physiological processes. Additionally, in bacterial pathogens, many exported proteins have functions in virulence. Consequently, the pathways that export proteins are commonly essential and/or are important for pathogenesis. Across bacteria, including mycobacteria, there are conserved protein export pathways: the general secretion (Sec) and the twin-arginine translocation (Tat) pathways. Both Sec and Tat pathways are essential to the viability of Mycobacterium tuberculosis and both also contribute to virulence (L. Rank and M. Braunstein, unpublished; 2 - 4 ). In addition to these conserved pathways, bacterial pathogens
Die Transfusionsassoziierte Akute Lungeninsuffizienz (TRALI) ist die häufigste tödliche Nebenwirkung der Transfusion von Blutprodukten und wird oft durch mittransfundierte leukozytenreaktive Antikörper (AK) induziert. AK gegen das Humane Neutrophilenantigen (HNA)-3a verursachen häufig schwere Fälle der TRALI. HNA-3a ist auf dem Großteil der Blutzelltypen exprimiert und entsteht durch einen Einzelnukleotidpolymorphismus im Gen des „choline transporter-like protein 2
Among the different families of transporter, only two occur ubiquitously in all classifications of organisms. These are the ATP-Binding Cassette (ABC) superfamily and the Major Facilitator Superfamily (MFS). The MFS transporters are single-polypeptide secondary carriers capable only of transporting small solutes in response to chemiosmotic ion gradients [(PUBMED:9529885), (PUBMED:9868370 ...
Conserved ER Protein Translocation Channel; Essential Subunit Of Sec61 Complex (Sec61p, Sbh1p, And Sss1p); Forms Channel For SRP-dependent Protein Import; With Sec63 Complex Allows SRP-independent Protein Import Into ER; Involved In Posttranslational Soluble Protein Import Into The ER, ERAD Of Soluble Substrates, And Misfolded Soluble Protein Export From The ER
GT:ID BAD57627.1 GT:GENE BAD57627.1 GT:PRODUCT putative transporter GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 2949754..2951109 GB:FROM 2949754 GB:TO 2951109 GB:DIRECTION + GB:PRODUCT putative transporter GB:PROTEIN_ID BAD57627.1 LENGTH 451 SQ:AASEQ MRMSSVLPQATDVDRRRVALATVVGTAVEWYDYFVYAAAAGLVFGTLFFEPAGPGFGTILSFLTVGISFLFRPLGAFLAGHFGDKVGRRPVLVTTLILMGTATALIGLLPTYEAIGIGAPLLLVLLRVLQGVSAGGEWGGAVLMAVEHAPRHRRGLFGAMPQIGVPIGLLLASAMMASMDALFPGEAFLDWGWRIPFLFSVVLIAVGAWVRRRVEESPVFAEIAERKEQTKAPVVDLFARFTPLVLLSALVFAGNSTVGYMTTGGYIQGYATNAEGLALDRGPVLWAVTASSLSWLLATFAAGWISDAIGRRATYIIGWCLQGVFVLTLFPLVNTGEVVLLGAGLVLLTLGLGFTYGAQSAWYTELFPASVRFSGVSISYAIGSIVGGAFAPTIAQWIQQSTGSSANVAYYLLAMTGVGLVGTVLLRDRKGIDLSPSNEAQQQTGIYAWEK GT:EXON 1,1-451:0, BL:SWS:NREP 1 BL:SWS:REP 15-,430,YHJE_ECOLI,7e-68,40.6,414/440, PROS 302-,318,PS00216,SUGAR_TRANSPORT_1,PDOC00190, TM:NTM 11 TM:REGION 31-,53, TM:REGION 56-,78, TM:REGION 90-,112, TM:REGION 114-,136, TM:REGION 162-,184, TM:REGION 189-,210, TM:REGION ...
GT:ID BAD57774.1 GT:GENE BAD57774.1 GT:PRODUCT putative transporter GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION complement(3108635..3109783) GB:FROM 3108635 GB:TO 3109783 GB:DIRECTION - GB:PRODUCT putative transporter GB:PROTEIN_ID BAD57774.1 LENGTH 382 SQ:AASEQ MSAPRPAPELTDRTGARLASTAAPVAGPEAAGPVPRGRTRSRAVIAFAVAVLALVALALASATIGQVPTTPAEVLGSVLHRIGLDWGPMPAHPAGDVTLWEVRFPRVLLAMLVGAALATAGALLQGVFANPLAEPGVIGVSSGAAVGAGATIVLGGAFVAAWSVAAAAFVAGLLTTMLVYVLARANGRTEVVTLVLTGVAINAFAGGLIAFLLFVASPAARDQIVFWQLGSLNGATWESVGVVAILTACGVAAAVLVAPRLDLLALGESAARHLGVDVERLRRNVIVIVAVLATAGVAFTGIIMFVGLIVPHLVRMIVGPAHRVLIPLSAVVGAVVLLAADVGARSLVDNADLPLGMLTSLVGGPFFFWLLRRTRARAGGWG GT:EXON 1,1-382:0, BL:SWS:NREP 1 BL:SWS:REP 173-,371,BTUC_VIBPA,1e-31,36.0,197/331, TM:NTM 9 TM:REGION 43-,65, TM:REGION 105-,127, TM:REGION 136-,158, TM:REGION 165-,187, TM:REGION 193-,215, TM:REGION 242-,264, TM:REGION 285-,307, TM:REGION 322-,344, TM:REGION 350-,371, SEG 22-,35,aapvagpeaagpvp, SEG 43-,62,aviafavavlalvalalasa, ...
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Plasma Membrane Permease; Mediates Uptake Of Glycerophosphoinositol And Glycerophosphocholine As Sources Of The Nutrients Inositol And Phosphate; Expression And Transport Rate Are Regulated By Phosphate And Inositol Availability
Cellular processesCellular processesToxin production and resistancedrug resistance MFS transporter, drug:H+ antiporter-2 (14 Spanner) (DHA2) family (TIGR00711; HMM-score: 64.3) ...
The Respiratory System. Cells continually use O2 & release CO2 Respiratory system designed for gas exchange Cardiovascular system transports gases in blood Failure of either system rapid cell death from O2 starvation. Nose -- Internal Structures. entrance - external nares...