TQSA_ECOLI
ID TQSA_ECOLI Reviewed; 344 AA.
AC P0AFS5; P77535;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=AI-2 transport protein TqsA;
DE AltName: Full=Transport of quorum-sensing signal protein;
GN Name=tqsA; Synonyms=ydgG; OrderedLocusNames=b1601, JW1593;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
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).
RN [5]
RP FUNCTION IN AI-2 TRANSPORT AND BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=16385049; DOI=10.1128/jb.188.2.587-598.2006;
RA Herzberg M., Kaye I.K., Peti W., Wood T.K.;
RT "YdgG (TqsA) controls biofilm formation in Escherichia coli K-12 through
RT autoinducer 2 transport.";
RL J. Bacteriol. 188:587-598(2006).
CC -!- FUNCTION: Controls the transport of the quorum-sensing signal AI-2
CC either by enhancing its secretion or inhibiting its uptake and
CC consequently represses biofilm formation and motility and affects the
CC global gene expression in biofilms. {ECO:0000269|PubMed:16385049}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Cells have a decreased extracellular and
CC increased intracellular concentration of AI-2. Deletion of tqsA results
CC in a 7000-fold increase in biofilm thickness and 574-fold increase in
CC biomass in flow cells. Deletion of tqsA increases cell motility by
CC increasing transcription of flagellar genes. The tqsA deletion mutant
CC shows higher resistance toward crystal violet, spectinomycin,
CC streptomycin sulfate, 2,6-dichloroquinone-4-chloroimide,
CC chloramphenicol and amoxicillin. {ECO:0000269|PubMed:16385049}.
CC -!- SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC74673.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15335.1; -; Genomic_DNA.
DR PIR; C64916; C64916.
DR RefSeq; NP_416118.1; NC_000913.3.
DR RefSeq; WP_001118241.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P0AFS5; -.
DR BioGRID; 4260647; 14.
DR STRING; 511145.b1601; -.
DR TCDB; 2.A.86.1.4; the autoinducer-2 exporter (ai-2e) family (formerly the perm family, tc #9,b,22).
DR PaxDb; P0AFS5; -.
DR PRIDE; P0AFS5; -.
DR EnsemblBacteria; AAC74673; AAC74673; b1601.
DR EnsemblBacteria; BAA15335; BAA15335; BAA15335.
DR GeneID; 946142; -.
DR KEGG; ecj:JW1593; -.
DR KEGG; eco:b1601; -.
DR PATRIC; fig|1411691.4.peg.661; -.
DR EchoBASE; EB3687; -.
DR eggNOG; COG0628; Bacteria.
DR HOGENOM; CLU_031275_0_3_6; -.
DR InParanoid; P0AFS5; -.
DR OMA; QEDPTDA; -.
DR PhylomeDB; P0AFS5; -.
DR BioCyc; EcoCyc:G6859-MON; -.
DR BioCyc; MetaCyc:G6859-MON; -.
DR PRO; PR:P0AFS5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:1905887; P:autoinducer AI-2 transmembrane transport; IMP:EcoCyc.
DR GO; GO:0009372; P:quorum sensing; IMP:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR002549; AI-2E-like.
DR PANTHER; PTHR21716; PTHR21716; 1.
DR Pfam; PF01594; AI-2E_transport; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Quorum sensing;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..344
FT /note="AI-2 transport protein TqsA"
FT /id="PRO_0000148297"
FT TOPO_DOM 1..4
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..61
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..197
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..257
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..316
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 344 AA; 37543 MW; 9DFFAFCD1480C482 CRC64;
MAKPIITLNG LKIVIMLGML VIILCGIRFA AEIIVPFILA LFIAVILNPL VQHMVRWRVP
RVLAVSILMT IIVMAMVLLL AYLGSALNEL TRTLPQYRNS IMTPLQALEP LLQRVGIDVS
VDQLAHYIDP NAAMTLLTNL LTQLSNAMSS IFLLLLTVLF MLLEVPQLPG KFQQMMARPV
EGMAAIQRAI DSVSHYLVLK TAISIITGLV AWAMLAALDV RFAFVWGLLA FALNYIPNIG
SVLAAIPPIA QVLVFNGFYE ALLVLAGYLL INLVFGNILE PRIMGRGLGL STLVVFLSLI
FWGWLLGPVG MLLSVPLTII VKIALEQTAG GQSIAVLLSD LNKE
