BTST_ECOLI
ID BTST_ECOLI Reviewed; 716 AA.
AC P39396; Q2M5W2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pyruvate/proton symporter BtsT {ECO:0000305};
DE AltName: Full=Brenztraubensaure transporter {ECO:0000303|PubMed:29061664};
DE AltName: Full=Pyruvate/H(+) symporter {ECO:0000303|PubMed:29061664};
GN Name=btsT {ECO:0000303|PubMed:29061664}; Synonyms=yjiY;
GN OrderedLocusNames=b4354, JW5791;
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 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 SUBCELLULAR LOCATION, AND 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 OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
RN [6]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22685278; DOI=10.1128/jb.00409-12;
RA Kraxenberger T., Fried L., Behr S., Jung K.;
RT "First insights into the unexplored two-component system YehU/YehT in
RT Escherichia coli.";
RL J. Bacteriol. 194:4272-4284(2012).
RN [7]
RP FUNCTION, INTERACTION WITH BTSS AND YPDA, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24659770; DOI=10.1128/jb.01554-14;
RA Behr S., Fried L., Jung K.;
RT "Identification of a novel nutrient-sensing histidine kinase/response
RT regulator network in Escherichia coli.";
RL J. Bacteriol. 196:2023-2029(2014).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=29061664; DOI=10.1128/jb.00599-17;
RA Kristoficova I., Vilhena C., Behr S., Jung K.;
RT "BtsT - a novel and specific pyruvate/H+ symporter in Escherichia coli.";
RL J. Bacteriol. 200:E00599-E00599(2018).
CC -!- FUNCTION: Transports pyruvate with a high affinity and specificity. The
CC process is driven by the proton motive force (PubMed:29061664). Under
CC nutrient limiting conditions, mediates the uptake of pyruvate, thus
CC enabling it to be used as a carbon source for the growth and survival
CC (PubMed:29061664). Part of a nutrient-sensing regulatory network
CC composed of the two-component regulatory systems BtsS/BtsR and
CC YpdA/YpdB, and their respective target proteins, BtsT and YhjX
CC (PubMed:24659770). {ECO:0000269|PubMed:24659770,
CC ECO:0000269|PubMed:29061664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in);
CC Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:29061664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64721;
CC Evidence={ECO:0000269|PubMed:29061664};
CC -!- ACTIVITY REGULATION: Transport is inhibited by the protonophores 2,4-
CC dinitrophenol (DNP) and carbonyl cyanide m-chlorophenyl hydrazone
CC (CCCP), but not by ionophores such as valinomycin, nonactin and
CC nigericin. {ECO:0000269|PubMed:29061664}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.5 uM for pyruvate {ECO:0000269|PubMed:29061664};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:29061664};
CC -!- SUBUNIT: Interacts with BtsS and YpdA. {ECO:0000269|PubMed:24659770}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:22685278, ECO:0000269|PubMed:29061664}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:29061664}.
CC -!- INDUCTION: Strongly induced at the onset of the stationary-growth
CC phase. Expression is dependent on the BtsS/BtsR two-component
CC regulatory system, and on cAMP and the cAMP receptor protein (CRP).
CC Repressed by LeuO. Monocistronic operon. Regulated at post-
CC transcriptional level by CsrA (PubMed:24659770).
CC {ECO:0000269|PubMed:19429622, ECO:0000269|PubMed:22685278,
CC ECO:0000269|PubMed:24659770}.
CC -!- SIMILARITY: Belongs to the peptide transporter carbon starvation (CstA)
CC (TC 2.A.114) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97251.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97251.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77310.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78344.1; -; Genomic_DNA.
DR PIR; S56580; S56580.
DR RefSeq; NP_418774.2; NC_000913.3.
DR RefSeq; WP_001299714.1; NZ_LN832404.1.
DR AlphaFoldDB; P39396; -.
DR BioGRID; 4261745; 187.
DR DIP; DIP-12649N; -.
DR IntAct; P39396; 2.
DR STRING; 511145.b4354; -.
DR jPOST; P39396; -.
DR PaxDb; P39396; -.
DR PRIDE; P39396; -.
DR EnsemblBacteria; AAC77310; AAC77310; b4354.
DR EnsemblBacteria; BAE78344; BAE78344; BAE78344.
DR GeneID; 948914; -.
DR KEGG; ecj:JW5791; -.
DR KEGG; eco:b4354; -.
DR PATRIC; fig|1411691.4.peg.2332; -.
DR EchoBASE; EB2472; -.
DR eggNOG; COG1966; Bacteria.
DR HOGENOM; CLU_010531_2_0_6; -.
DR InParanoid; P39396; -.
DR OMA; GTISGFH; -.
DR PhylomeDB; P39396; -.
DR BioCyc; EcoCyc:G7942-MON; -.
DR BioCyc; MetaCyc:G7942-MON; -.
DR PRO; PR:P39396; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005477; F:pyruvate secondary active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0031669; P:cellular response to nutrient levels; IEP:EcoCyc.
DR GO; GO:0009267; P:cellular response to starvation; TAS:EcoCyc.
DR GO; GO:0006849; P:plasma membrane pyruvate transport; IDA:EcoCyc.
DR InterPro; IPR025299; CstA_C.
DR InterPro; IPR003706; CstA_N.
DR Pfam; PF02554; CstA; 1.
DR Pfam; PF13722; CstA_5TM; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..716
FT /note="Pyruvate/proton symporter BtsT"
FT /id="PRO_0000190050"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29061664"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..30
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..119
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..191
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..257
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..326
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..484
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..568
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..668
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT REGION 696..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 77324 MW; 664E7B6169F15B4D CRC64;
MDTKKIFKHI PWVILGIIGA FCLAVVALRR GEHISALWIV VASVSVYLVA YRYYSLYIAQ
KVMKLDPTRA TPAVINNDGL NYVPTNRYVL FGHHFAAIAG AGPLVGPVLA AQMGYLPGTL
WLLAGVVLAG AVQDFMVLFI SSRRNGASLG EMIKEEMGPV PGTIALFGCF LIMIIILAVL
ALIVVKALAE SPWGVFTVCS TVPIALFMGI YMRFIRPGRV GEVSVIGIVL LVASIYFGGV
IAHDPYWGPA LTFKDTTITF ALIGYAFVSA LLPVWLILAP RDYLATFLKI GVIVGLALGI
VVLNPELKMP AMTQYIDGTG PLWKGALFPF LFITIACGAV SGFHALISSG TTPKLLANET
DARFIGYGAM LMESFVAIMA LVAASIIEPG LYFAMNTPPA GLGITMPNLH EMGGENAPII
MAQLKDVTAH AAATVSSWGF VISPEQILQT AKDIGEPSVL NRAGGAPTLA VGIAHVFHKV
LPMADMGFWY HFGILFEALF ILTALDAGTR SGRFMLQDLL GNFIPFLKKT DSLVAGIIGT
AGCVGLWGYL LYQGVVDPLG GVKSLWPLFG ISNQMLAAVA LVLGTVVLIK MKRTQYIWVT
VVPAVWLLIC TTWALGLKLF STNPQMEGFF YMASQYKEKI ANGTDLTAQQ IANMNHIVVN
NYTNAGLSIL FLIVVYSIIF YGFKTWLAVR NSDKRTDKET PYVPIPEGGV KISSHH
