Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein‐dependent transport systems
The MalG protein is needed for the transport of maltose in Escherichia coli K12. We present the sequence of gene malG. The deduced amino acid sequence corresponds to a protein of 296 amino acid residues (mol. wt. = 32 188 daltons). This protein is largely hydrophobic (hydrophobic index = 0.83) and i...
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| Veröffentlicht in: | The EMBO journal 1985-09, Vol.4 (9), p.2287-2293 |
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| description | The MalG protein is needed for the transport of maltose in Escherichia coli K12. We present the sequence of gene malG. The deduced amino acid sequence corresponds to a protein of 296 amino acid residues (mol. wt. = 32 188 daltons). This protein is largely hydrophobic (hydrophobic index = 0.83) and is thus presumably an integral inner membrane protein which could span the membrane through six hydrophobic segments. We provide direct evidence from fusion proteins for the translation frame and we also identified the in vitro made MalG protein. We have found a sequence which is highly conserved between MalG and MalF, the other integral inner membrane protein of the maltose transport system. This conserved sequence is also present in all known integral membrane proteins of binding protein‐dependent transport systems, always at the same distance (approximately 90 residues) from their COOH terminus. We discuss briefly this finding. |
| doi_str_mv | 10.1002/j.1460-2075.1985.tb03928.x |
| format | Article |
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We present the sequence of gene malG. The deduced amino acid sequence corresponds to a protein of 296 amino acid residues (mol. wt. = 32 188 daltons). This protein is largely hydrophobic (hydrophobic index = 0.83) and is thus presumably an integral inner membrane protein which could span the membrane through six hydrophobic segments. We provide direct evidence from fusion proteins for the translation frame and we also identified the in vitro made MalG protein. We have found a sequence which is highly conserved between MalG and MalF, the other integral inner membrane protein of the maltose transport system. This conserved sequence is also present in all known integral membrane proteins of binding protein‐dependent transport systems, always at the same distance (approximately 90 residues) from their COOH terminus. We discuss briefly this finding.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1985.tb03928.x</identifier><identifier>PMID: 3000770</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Amino Acid Sequence ; ATP-Binding Cassette Transporters ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Carrier Proteins - genetics ; Cloning, Molecular ; DNA Restriction Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Fundamental and applied biological sciences. Psychology ; gene expression ; Genes ; Genes, Bacterial ; Genetics ; Genotype ; Maltose-Binding Proteins ; membrane proteins ; Membrane Proteins - genetics ; Microbiology ; Monosaccharide Transport Proteins ; nucleotide sequence ; Plasmids ; Sequence Homology, Nucleic Acid ; Species Specificity</subject><ispartof>The EMBO journal, 1985-09, Vol.4 (9), p.2287-2293</ispartof><rights>1985 European Molecular Biology Organization</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4538-8bcc5adb4cfb0275226bbce79a0c68b43f4c1dc88568abc3a3ed512de18ba8733</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC554499/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC554499/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8510433$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3000770$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dassa, E.</creatorcontrib><creatorcontrib>Hofnung, M.</creatorcontrib><title>Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein‐dependent transport systems</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>The MalG protein is needed for the transport of maltose in Escherichia coli K12. We present the sequence of gene malG. The deduced amino acid sequence corresponds to a protein of 296 amino acid residues (mol. wt. = 32 188 daltons). This protein is largely hydrophobic (hydrophobic index = 0.83) and is thus presumably an integral inner membrane protein which could span the membrane through six hydrophobic segments. We provide direct evidence from fusion proteins for the translation frame and we also identified the in vitro made MalG protein. We have found a sequence which is highly conserved between MalG and MalF, the other integral inner membrane protein of the maltose transport system. This conserved sequence is also present in all known integral membrane proteins of binding protein‐dependent transport systems, always at the same distance (approximately 90 residues) from their COOH terminus. We discuss briefly this finding.</description><subject>Amino Acid Sequence</subject><subject>ATP-Binding Cassette Transporters</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - genetics</subject><subject>Cloning, Molecular</subject><subject>DNA Restriction Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene expression</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>Genetics</subject><subject>Genotype</subject><subject>Maltose-Binding Proteins</subject><subject>membrane proteins</subject><subject>Membrane Proteins - genetics</subject><subject>Microbiology</subject><subject>Monosaccharide Transport Proteins</subject><subject>nucleotide sequence</subject><subject>Plasmids</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Species Specificity</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1u1DAUhSMEKkPhEZAshNgl2LGdOJVYlGooP0UsgLVlOzdTj2I7xBna2bFkyTPyJDhMNIIVYuUrnXOse8-XZU8ILgjG5fNtQViF8xLXvCCN4MWkMW1KUdzeyVZH6W62wmVFckZEcz97EOMWY8xFTU6yE5rGusar7PtH-LIDbwCFDm3AA3Kqv0TWo3WBTOgtekfKM3QdXOjDxkJEGqYbAJ8sE2xG1SMHTo8qJU1wQ_Dgp4i6MTikrW-t36BhDBNY__PbjxYG8G1yoCkl4hDGCcV9nMDFh9m9TvURHi3vafb51frTxev86sPlm4vzq9wwTkUutDFctZqZTuOy5mVZaW2gbhQ2ldCMdsyQ1gjBK6G0oYpCy0nZAhFaiZrS0-zF4d9hpx20Ji2TjpDDaJ0a9zIoK_9WvL2Wm_BVcs5Y06T8syU_htRcnKSz0UDfpwbCLsq64hQnJv80EkZ5TWqWjGcHoxlDjCN0x2UIljNvuZUzVDlDlTNvufCWtyn8-M9zjtEFcNKfLrqKRvVdqt3YeLQJTjCjcyvnB9uN7WH_HwvI9fuXb3_P9BfKP82H</recordid><startdate>198509</startdate><enddate>198509</enddate><creator>Dassa, E.</creator><creator>Hofnung, M.</creator><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>198509</creationdate><title>Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein‐dependent transport systems</title><author>Dassa, E. ; Hofnung, M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4538-8bcc5adb4cfb0275226bbce79a0c68b43f4c1dc88568abc3a3ed512de18ba8733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Amino Acid Sequence</topic><topic>ATP-Binding Cassette Transporters</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - genetics</topic><topic>Cloning, Molecular</topic><topic>DNA Restriction Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene expression</topic><topic>Genes</topic><topic>Genes, Bacterial</topic><topic>Genetics</topic><topic>Genotype</topic><topic>Maltose-Binding Proteins</topic><topic>membrane proteins</topic><topic>Membrane Proteins - genetics</topic><topic>Microbiology</topic><topic>Monosaccharide Transport Proteins</topic><topic>nucleotide sequence</topic><topic>Plasmids</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dassa, E.</creatorcontrib><creatorcontrib>Hofnung, M.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dassa, E.</au><au>Hofnung, M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein‐dependent transport systems</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1985-09</date><risdate>1985</risdate><volume>4</volume><issue>9</issue><spage>2287</spage><epage>2293</epage><pages>2287-2293</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The MalG protein is needed for the transport of maltose in Escherichia coli K12. We present the sequence of gene malG. The deduced amino acid sequence corresponds to a protein of 296 amino acid residues (mol. wt. = 32 188 daltons). This protein is largely hydrophobic (hydrophobic index = 0.83) and is thus presumably an integral inner membrane protein which could span the membrane through six hydrophobic segments. We provide direct evidence from fusion proteins for the translation frame and we also identified the in vitro made MalG protein. We have found a sequence which is highly conserved between MalG and MalF, the other integral inner membrane protein of the maltose transport system. This conserved sequence is also present in all known integral membrane proteins of binding protein‐dependent transport systems, always at the same distance (approximately 90 residues) from their COOH terminus. We discuss briefly this finding.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>3000770</pmid><doi>10.1002/j.1460-2075.1985.tb03928.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence ATP-Binding Cassette Transporters Bacteriology Base Sequence Biological and medical sciences Carrier Proteins - genetics Cloning, Molecular DNA Restriction Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology gene expression Genes Genes, Bacterial Genetics Genotype Maltose-Binding Proteins membrane proteins Membrane Proteins - genetics Microbiology Monosaccharide Transport Proteins nucleotide sequence Plasmids Sequence Homology, Nucleic Acid Species Specificity |
| title | Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein‐dependent transport systems |
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