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PMID: 2022620 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli.

Journal of bacteriology ·Vol. 173 ·No. 10 ·1991-05-00 ·Pages 3231-4

Sarsero JP, Wookey PJ, Gollnick P, Yanofsky C, Pittard AJ

Abstract

The nucleotide sequence of tnaB of the tryptophanase operon of Escherichia coli is presented. TnaB is a tryptophan-specific permease that is homologous to Mtr, a second tryptophan-specific permease, and to TyrP, a tyrosine-specific permease. Each member of this family appears to contain 11 membrane-spanning domains.

MeSH Terms
Amino Acid Sequence Amino Acid Transport Systems Amino Acids/metabolism Bacterial Proteins/genetics Base Sequence Carrier Proteins/genetics Cloning, Molecular Escherichia coli/metabolism Escherichia coli Proteins Genes, Bacterial Membrane Proteins/genetics Membrane Transport Proteins/genetics Molecular Sequence Data
Chemicals
Amino Acid Transport Systems Amino Acids Bacterial Proteins Carrier Proteins Escherichia coli Proteins Membrane Proteins Membrane Transport Proteins TnaB protein, E coli
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Sarsero J P
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
Wookey P J
Gollnick P
Yanofsky C
Pittard A J
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27 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.173.10.3231-3234.1991
Published
1991-05-00
Pages
3231-4
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC207920
Subset
IM
Databases
GENBANK
M55488, M55489, M55490, M55491, M55492, M55493, M55494, M59914, M81169, X52418
External Links
PubMed source DOI: 10.1128/jb.173.10.3231-3234.1991 PMC Full Text View journal details
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