TNAB_ECO57
ID TNAB_ECO57 Reviewed; 415 AA.
AC Q8XB33;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Low affinity tryptophan permease;
GN Name=tnaB; OrderedLocusNames=Z5204, ECs4646;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Involved in tryptophan transport across the cytoplasmic
CC membrane. Plays a role in transporting tryptophan which is to be used
CC catabolically (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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; AE005174; AAG58909.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38069.1; -; Genomic_DNA.
DR PIR; A86056; A86056.
DR PIR; F91209; F91209.
DR RefSeq; NP_312673.1; NC_002695.1.
DR RefSeq; WP_000131901.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XB33; -.
DR SMR; Q8XB33; -.
DR STRING; 155864.EDL933_5034; -.
DR EnsemblBacteria; AAG58909; AAG58909; Z5204.
DR EnsemblBacteria; BAB38069; BAB38069; ECs_4646.
DR GeneID; 915392; -.
DR KEGG; ece:Z5204; -.
DR KEGG; ecs:ECs_4646; -.
DR PATRIC; fig|386585.9.peg.4855; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_038102_2_1_6; -.
DR OMA; FAYVSHM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 3: Inferred from homology;
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_0000093801"
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"
SQ SEQUENCE 415 AA; 45196 MW; 4F8502CC77349702 CRC64;
MTDQAEKKHS AFWGVMVIAG TVIGGGMFAL PVDLAGAWFF WGAFILIIAW FSMLHSGLLL
LEANLNYPVG SSFNTITKDL IGNTWNIISG ITVAFVLYIL TYAYISANGA IISETISMNL
GYHANPRIVG ICTAIFVASV LWISSLAASR ITSLFLGLKI ISFVIVFGSF FFLVDYSILR
DATSSTAGTS YFPYIFMALP VCLASFGFHG NIPSLIICYG KRKDKLIKSV VFGSLLALVI
YLFWLYCTMG NIPRESFKAI ISSGGNVDSL VKSFLGTKQH GIIEFCLLVF SNLAVASSFF
GVTLGLFDYL ADLFKIDNSH GGRFKTVLLT FLPPALLYLI FPNGFIYGIG GAGLCATIWA
VIIPAVLAIK ARKKFPNQMF TVWGGNLIPA IVILFGITVI LCWFGNVFNV LPKFG
