TSX_ECOLI
ID TSX_ECOLI Reviewed; 294 AA.
AC P0A927; P22786; Q2MC15;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Nucleoside-specific channel-forming protein Tsx {ECO:0000305};
DE Flags: Precursor;
GN Name=tsx {ECO:0000303|PubMed:791677}; Synonyms=nupA;
GN OrderedLocusNames=b0411, JW0401;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2265760; DOI=10.1016/0378-1119(90)90341-n;
RA Bremer E., Middendorf A., Martinussen J., Valentin-Hansen P.;
RT "Analysis of the tsx gene, which encodes a nucleoside-specific channel-
RT forming protein (Tsx) in the outer membrane of Escherichia coli.";
RL Gene 96:59-65(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 269-284, AND PHAGE RESISTANT MUTANT.
RC STRAIN=K12;
RX PubMed=2199819; DOI=10.1007/bf00259416;
RA Maier C., Middendorf A., Bremer E.;
RT "Analysis of a mutated phage T6 receptor protein of Escherichia coli K
RT 12.";
RL Mol. Gen. Genet. 221:491-494(1990).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=791677; DOI=10.1016/0014-5793(76)80737-5;
RA Hantke K.;
RT "Phage T6--colicin K receptor and nucleoside transport in Escherichia
RT coli.";
RL FEBS Lett. 70:109-112(1976).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2458926; DOI=10.1111/j.1432-1033.1988.tb14333.x;
RA Benz R., Schmid A., Maier C., Bremer E.;
RT "Characterization of the nucleoside-binding site inside the Tsx channel of
RT Escherichia coli outer membrane. Reconstitution experiments with lipid
RT bilayer membranes.";
RL Eur. J. Biochem. 176:699-705(1988).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=3276691; DOI=10.1016/s0021-9258(18)69233-6;
RA Maier C., Bremer E., Schmid A., Benz R.;
RT "Pore-forming activity of the Tsx protein from the outer membrane of
RT Escherichia coli. Demonstration of a nucleoside-specific binding site.";
RL J. Biol. Chem. 263:2493-2499(1988).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=EPI100;
RX PubMed=28351921; DOI=10.1128/mbio.00290-17;
RA Ruhe Z.C., Nguyen J.Y., Xiong J., Koskiniemi S., Beck C.M., Perkins B.R.,
RA Low D.A., Hayes C.S.;
RT "CdiA effectors use modular receptor-binding domains to recognize target
RT bacteria.";
RL MBio 8:0-0(2017).
CC -!- FUNCTION: Functions as substrate-specific channel for nucleosides and
CC deoxynucleosides (PubMed:791677, PubMed:3276691, PubMed:2458926). Has a
CC greater affinity for deoxynucleosides than for nucleosides, and does
CC not transport free bases (PubMed:2458926). In addition, constitutes the
CC receptor for colicin K and phage T6 (PubMed:791677, PubMed:3276691).
CC {ECO:0000269|PubMed:2458926, ECO:0000269|PubMed:3276691,
CC ECO:0000269|PubMed:791677}.
CC -!- FUNCTION: (Microbial infection) Serves as a receptor for CdiA-STECO31,
CC required for adhesion between E.coli expressing CdiA-STECO31 and this
CC strain. {ECO:0000269|PubMed:28351921}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:3276691,
CC ECO:0000269|PubMed:791677}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:2458926, ECO:0000305|PubMed:3276691}.
CC -!- DISRUPTION PHENOTYPE: Loss of susceptibility to contact-dependent
CC growth inhibition by CdiA-STECO31. {ECO:0000269|PubMed:28351921}.
CC -!- SIMILARITY: Belongs to the nucleoside-specific channel-forming outer
CC membrane porin (Tsx) (TC 1.B.10) family. {ECO:0000305}.
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DR EMBL; M57685; AAA24701.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40167.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73514.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76191.1; -; Genomic_DNA.
DR PIR; JQ0798; JQ0798.
DR RefSeq; NP_414945.1; NC_000913.3.
DR RefSeq; WP_001295328.1; NZ_STEB01000007.1.
DR PDB; 1TLW; X-ray; 3.10 A; A/B=23-294.
DR PDB; 1TLY; X-ray; 3.01 A; A/B=23-294.
DR PDB; 1TLZ; X-ray; 3.10 A; A/B=23-294.
DR PDBsum; 1TLW; -.
DR PDBsum; 1TLY; -.
DR PDBsum; 1TLZ; -.
DR AlphaFoldDB; P0A927; -.
DR SMR; P0A927; -.
DR BioGRID; 4263182; 129.
DR STRING; 511145.b0411; -.
DR DrugBank; DB04485; Thymidine.
DR DrugBank; DB02745; Uridine.
DR TCDB; 1.B.10.1.1; the nucleoside-specific channel-forming outer membrane porin (tsx) family.
DR jPOST; P0A927; -.
DR PaxDb; P0A927; -.
DR PRIDE; P0A927; -.
DR EnsemblBacteria; AAC73514; AAC73514; b0411.
DR EnsemblBacteria; BAE76191; BAE76191; BAE76191.
DR GeneID; 67416514; -.
DR GeneID; 946242; -.
DR KEGG; ecj:JW0401; -.
DR KEGG; eco:b0411; -.
DR PATRIC; fig|1411691.4.peg.1866; -.
DR EchoBASE; EB1028; -.
DR eggNOG; COG3248; Bacteria.
DR HOGENOM; CLU_073836_0_0_6; -.
DR OMA; KSTGWGY; -.
DR PhylomeDB; P0A927; -.
DR BioCyc; EcoCyc:EG11035-MON; -.
DR BioCyc; MetaCyc:EG11035-MON; -.
DR EvolutionaryTrace; P0A927; -.
DR PRO; PR:P0A927; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0046930; C:pore complex; IDA:EcoCyc.
DR GO; GO:0015471; F:nucleoside-specific channel forming porin activity; IDA:EcoCyc.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015858; P:nucleoside transport; IDA:EcoCyc.
DR GO; GO:0046718; P:viral entry into host cell; IMP:EcoCyc.
DR Gene3D; 2.40.230.20; -; 1.
DR InterPro; IPR003055; Channel_Tsx.
DR InterPro; IPR018013; Channel_Tsx-like.
DR InterPro; IPR036777; Channel_Tsx-like_sf.
DR Pfam; PF03502; Channel_Tsx; 1.
DR PRINTS; PR01277; CHANNELTSX.
DR SUPFAM; SSF111364; SSF111364; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Membrane; Porin;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..294
FT /note="Nucleoside-specific channel-forming protein Tsx"
FT /id="PRO_0000025190"
FT VARIANT 276
FT /note="N -> Y (in phage resistant mutant)"
FT /evidence="ECO:0000269|PubMed:2199819"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 35..47
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:1TLY"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 121..133
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 156..173
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 180..198
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 201..213
FT /evidence="ECO:0007829|PDB:1TLY"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 247..260
FT /evidence="ECO:0007829|PDB:1TLY"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1TLY"
FT STRAND 282..294
FT /evidence="ECO:0007829|PDB:1TLY"
SQ SEQUENCE 294 AA; 33589 MW; AB801DC563552A5C CRC64;
MKKTLLAAGA VLALSSSFTV NAAENDKPQY LSDWWHQSVN VVGSYHTRFG PQIRNDTYLE
YEAFAKKDWF DFYGYADAPV FFGGNSDAKG IWNHGSPLFM EIEPRFSIDK LTNTDLSFGP
FKEWYFANNY IYDMGRNKDG RQSTWYMGLG TDIDTGLPMS LSMNVYAKYQ WQNYGAANEN
EWDGYRFKIK YFVPITDLWG GQLSYIGFTN FDWGSDLGDD SGNAINGIKT RTNNSIASSH
ILALNYDHWH YSVVARYWHD GGQWNDDAEL NFGNGNFNVR STGWGGYLVV GYNF
