TNAB_PROVU
ID TNAB_PROVU Reviewed; 417 AA.
AC P28785;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Low affinity tryptophan permease;
GN Name=tnaB; Synonyms=trpP;
OS Proteus vulgaris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400314; DOI=10.1016/s0021-9258(19)88653-2;
RA Kamath A.V., Yanofsky C.;
RT "Characterization of the tryptophanase operon of Proteus vulgaris. Cloning,
RT nucleotide sequence, amino acid homology, and in vitro synthesis of the
RT leader peptide and regulatory analysis.";
RL J. Biol. Chem. 267:19978-19985(1992).
CC -!- FUNCTION: Involved in tryptophan transport across the cytoplasmic
CC membrane. Plays a role in transporting tryptophan which is to be used
CC catabolically.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By tryptophan. Is subject to catabolic repression.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC Mtr/TnaB/TyrP permease subfamily. {ECO:0000305}.
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DR EMBL; M93277; AAA25665.1; -; Genomic_DNA.
DR PIR; C44038; C44038.
DR AlphaFoldDB; P28785; -.
DR SMR; P28785; -.
DR STRING; 585.DR95_2913; -.
DR eggNOG; COG0814; Bacteria.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR018227; Amino_acid_transport_2.
DR InterPro; IPR013061; Trp/try_permease_CS.
DR InterPro; IPR013059; Trp_tyr_transpt.
DR PANTHER; PTHR46997; PTHR46997; 1.
DR Pfam; PF03222; Trp_Tyr_perm; 1.
DR PRINTS; PR00166; AROAAPRMEASE.
DR TIGRFAMs; TIGR00837; araaP; 1.
DR PROSITE; PS00594; AROMATIC_AA_PERMEASE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport; Tryptophan catabolism.
FT CHAIN 1..417
FT /note="Low affinity tryptophan permease"
FT /id="PRO_0000093802"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 417 AA; 46273 MW; 9EA4E61E6AE8CAE1 CRC64;
MENTSVNKEP SIIVGGFVLG GAMIGAGMFS LPTIMSGAWF INSLFILFIV CFFMFHSGIY
ILECISKYGA GTNYFDISKE LLPKWACYIA NASLIFVLYI LIYAYISAAG SIIYEASLLY
GINFNLRAIF FIFTIALGAT IWWGGACASR LTSIFLFIKI VLFILAFSGL FFKAKGDLLF
SATFAGKSQL YLYPFIFIII PYAITSFGYH GNVCSLYKLY NQNERKVVKS CIIGCLLALV
IYLLWMIGTM GNLPREQFIT IIQKGGNLDA FIDSLYTVLN SKYIEGFLLW FSISAVFCSF
LGVAIGLFDY ILASLKFKDN KTGRLKSGVL CFTPPLLLCL FFPNGFLIAI AYAGTAACVW
AIICPAVMAL KARQKFPNSG FKVWGGKKLI YAVIAFGVVG IICQSWRNLI YCLFIVK