TNAB_ECOLI
ID TNAB_ECOLI Reviewed; 415 AA.
AC P23173; Q2M823; Q2M825;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Low affinity tryptophan permease;
GN Name=tnaB; Synonyms=trpP; OrderedLocusNames=b3709, JW5619/JW5622;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2022620; DOI=10.1128/jb.173.10.3231-3234.1991;
RA Sarsero J.P., Wookey P.J., Gollnick P.D., Yanofsky C., Pittard A.J.;
RT "A new family of integral membrane proteins involved in transport of
RT aromatic amino acids in Escherichia coli.";
RL J. Bacteriol. 173:3231-3234(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC STRAIN=K12;
RX PubMed=6268608; DOI=10.1128/jb.147.3.787-796.1981;
RA Deeley M.C., Yanofsky C.;
RT "Nucleotide sequence of the structural gene for tryptophanase of
RT Escherichia coli K-12.";
RL J. Bacteriol. 147:787-796(1981).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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}.
CC -!- CAUTION: In strain W3110, the sequence is interrupted by the insertion
CC of an IS5 element between positions 291 and 292. {ECO:0000305}.
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DR EMBL; M59914; AAA62792.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62060.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76732.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77581.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP009048; BAE77583.1; ALT_SEQ; Genomic_DNA.
DR EMBL; K00032; AAA24677.1; -; Genomic_DNA.
DR PIR; A39412; A39412.
DR RefSeq; NP_418165.1; NC_000913.3.
DR RefSeq; WP_000131925.1; NZ_LN832404.1.
DR AlphaFoldDB; P23173; -.
DR SMR; P23173; -.
DR STRING; 511145.b3709; -.
DR TCDB; 2.A.42.1.3; the hydroxy/aromatic amino acid permease (haaap) family.
DR jPOST; P23173; -.
DR PaxDb; P23173; -.
DR PRIDE; P23173; -.
DR EnsemblBacteria; AAC76732; AAC76732; b3709.
DR EnsemblBacteria; BAE77581; BAE77581; BAE77581.
DR EnsemblBacteria; BAE77583; BAE77583; BAE77583.
DR GeneID; 948220; -.
DR KEGG; ecj:JW5619; -.
DR KEGG; ecj:JW5622; -.
DR KEGG; eco:b3709; -.
DR PATRIC; fig|1411691.4.peg.2992; -.
DR EchoBASE; EB0999; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_1956281_0_0_6; -.
DR InParanoid; P23173; -.
DR OMA; FAYVSHM; -.
DR PhylomeDB; P23173; -.
DR BioCyc; EcoCyc:TNAB-MON; -.
DR BioCyc; MetaCyc:TNAB-MON; -.
DR PRO; PR:P23173; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IMP:EcoCyc.
DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Tryptophan catabolism.
FT CHAIN 1..415
FT /note="Low affinity tryptophan permease"
FT /id="PRO_0000093800"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..127
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..191
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..286
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..415
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="D -> V (in Ref. 5; AAA24677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45211 MW; 1E34C7DE3DF6E9D9 CRC64;
MTDQAEKKHS AFWGVMVIAG TVIGGGMFAL PVDLAGAWFF WGAFILIIAW FSMLHSGLLL
LEANLNYPVG SSFNTITKDL IGNTWNIISG ITVAFVLYIL TYAYISANGA IISETISMNL
GYHANPRIVG ICTAIFVASV LWLSSLAASR ITSLFLGLKI ISFVIVFGSF FFQVDYSILR
DATSSTAGTS YFPYIFMALP VCLASFGFHG NIPSLIICYG KRKDKLIKSV VFGSLLALVI
YLFWLYCTMG NIPRESFKAI ISSGGNVDSL VKSFLGTKQH GIIEFCLLVF SNLAVASSFF
GVTLGLFDYL ADLFKIDNSH GGRFKTVLLT FLPPALLYLI FPNGFIYGIG GAGLCATIWA
VIIPAVLAIK ARKKFPNQMF TVWGGNLIPA IVILFGITVI LCWFGNVFNV LPKFG
