1992
DOI: 10.1111/j.1365-2958.1992.tb01444.x
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Identification and sequence of a Na+‐linked gene from the marine bacterium Alteromonas haloplanktis which functionally complements the dagA gene of Escherichia coli

Abstract: A 4.0 kb fragment from a plasmid genomic DNA library of the marine bacterium Alteromonas haloplanktis ATCC 19855 was found in the presence of Na+ to complement the dagA gene of Escherichia coli. We have completely sequenced this fragment and the position of the Na(+)-linked D-alanine glycine permease gene (dagA) on the fragment has been determined by complementation. The predicted carrier protein consists of 542 amino acid residues (M(r) 58,955). Its hydropathy profile suggests it is composed of eight transmem… Show more

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Cited by 15 publications
(11 citation statements)
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“…S2 in the supplemental material). The riboswitch has structural and sequence homology to other glycine riboswitches (28), and AA00167 belongs to the sodium/alanine symporter superfamily (35), which includes a known glycine transporter (34). We also observed high levels of an sRNA homologous to GcvB in A. actinomycetemcomitans biofilms.…”
Section: Discussionmentioning
confidence: 54%
“…S2 in the supplemental material). The riboswitch has structural and sequence homology to other glycine riboswitches (28), and AA00167 belongs to the sodium/alanine symporter superfamily (35), which includes a known glycine transporter (34). We also observed high levels of an sRNA homologous to GcvB in A. actinomycetemcomitans biofilms.…”
Section: Discussionmentioning
confidence: 54%
“…6) revealed 50% homology between Orf3 and the D-alanine permease (DagA) of the marine bacterium Alteromonas haloplanktis (26) and 71% homology between Orf1 and the YadQ protein of E. coli, whose function has not been defined (14). Low homologies to eukaryotic chloride channels and the Gef1 protein of Saccharomyces cerevisiae, were found; a relationship to iron and citrate has been found for this protein (10).…”
Section: Discussionmentioning
confidence: 99%
“…The search for similar proteins in the databases gave a few positive results. Several of them do not have a known function, but two of the other proteins are sodium/proton-dependent alanine carrier proteins (MacLeod & MacLeod, 1992;Kamata e t al., 1992). The transmembrane domains and the similarities to known proteins are indications of a possible amino acid carrier function for this protein.…”
mentioning
confidence: 99%