RHAT_ECOLI
ID RHAT_ECOLI Reviewed; 344 AA.
AC P27125; Q2M8K4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=L-rhamnose-proton symporter {ECO:0000255|HAMAP-Rule:MF_01532, ECO:0000305};
DE AltName: Full=L-rhamnose-H(+) transport protein {ECO:0000255|HAMAP-Rule:MF_01532, ECO:0000303|PubMed:1551902};
GN Name=rhaT {ECO:0000255|HAMAP-Rule:MF_01532, ECO:0000303|PubMed:2283027};
GN OrderedLocusNames=b3907, JW3878;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=1551902; DOI=10.1016/s0021-9258(19)50517-8;
RA Tate C.G., Muiry J.A.R., Henderson P.J.F.;
RT "Mapping, cloning, expression, and sequencing of the rhaT gene, which
RT encodes a novel L-rhamnose-H+ transport protein in Salmonella typhimurium
RT and Escherichia coli.";
RL J. Biol. Chem. 267:6923-6932(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1339463; DOI=10.1099/00221287-138-6-1109;
RA Garcia C., Baldoma L., Badia J., Aguilar J.;
RT "Nucleotide sequence of the rhaR-sodA interval specifying rhaT in
RT Escherichia coli.";
RL J. Gen. Microbiol. 138:1109-1116(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2283027; DOI=10.1016/0378-1097(90)90353-r;
RA Baldoma L., Badia J., Sweet G., Aguilar J.;
RT "Cloning, mapping and gene product identification of rhaT from Escherichia
RT coli K12.";
RL FEMS Microbiol. Lett. 60:103-107(1990).
RN [7]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1650346; DOI=10.1128/jb.173.16.5144-5150.1991;
RA Badia J., Gimenez R., Baldoma L., Barnes E., Fessner W.D., Aguilar J.;
RT "L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of
RT Escherichia coli adapted to grow on L-lyxose.";
RL J. Bacteriol. 173:5144-5150(1991).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8384447; DOI=10.1042/bj2900833;
RA Muiry J.A., Gunn T.C., McDonald T.P., Bradley S.A., Tate C.G.,
RA Henderson P.J.;
RT "Proton-linked L-rhamnose transport, and its comparison with L-fucose
RT transport in Enterobacteriaceae.";
RL Biochem. J. 290:833-842(1993).
RN [9]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8262918; DOI=10.1016/s0021-9258(19)74189-1;
RA Tate C.G., Henderson P.J.F.;
RT "Membrane topology of the L-rhamnose-H+ transport protein (RhaT) from
RT enterobacteria.";
RL J. Biol. Chem. 268:26850-26857(1993).
RN [10]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=8757746; DOI=10.1099/13500872-142-7-1833;
RA Via P., Badia J., Baldoma L., Obradors N., Aguilar J.;
RT "Transcriptional regulation of the Escherichia coli rhaT gene.";
RL Microbiology 142:1833-1840(1996).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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: Uptake of L-rhamnose across the cytoplasmic membrane with the
CC concomitant transport of protons into the cell (symport system)
CC (PubMed:2283027, PubMed:1551902, PubMed:8384447). Can also transport L-
CC mannose and L-lyxose, but at reduced rates (PubMed:8384447,
CC PubMed:1650346). {ECO:0000269|PubMed:1551902,
CC ECO:0000269|PubMed:1650346, ECO:0000269|PubMed:2283027,
CC ECO:0000269|PubMed:8384447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-rhamnopyranose(in) = H(+)(out) + L-
CC rhamnopyranose(out); Xref=Rhea:RHEA:29947, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:62346; Evidence={ECO:0000255|HAMAP-Rule:MF_01532,
CC ECO:0000269|PubMed:8384447};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29949;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01532,
CC ECO:0000269|PubMed:8384447, ECO:0000305|PubMed:1650346};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-mannopyranose(in) = H(+)(out) + L-
CC mannopyranose(out); Xref=Rhea:RHEA:70991, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37677; Evidence={ECO:0000269|PubMed:8384447};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70993;
CC Evidence={ECO:0000269|PubMed:8384447};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-lyxopyranose(in) = H(+)(out) + L-
CC lyxopyranose(out); Xref=Rhea:RHEA:29991, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:62321; Evidence={ECO:0000269|PubMed:8384447,
CC ECO:0000305|PubMed:1650346};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29993;
CC Evidence={ECO:0000269|PubMed:8384447, ECO:0000305|PubMed:1650346};
CC -!- ACTIVITY REGULATION: Inhibited by protonophores and ionophores, but is
CC insensitive to the thiol reagent N-ethylmaleimide or cytochalasin B.
CC {ECO:0000269|PubMed:8384447}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=12 nmol/min/mg enzyme {ECO:0000269|PubMed:8384447};
CC pH dependence:
CC Optimum pH is 7 for L-rhamnose transport.
CC {ECO:0000269|PubMed:8384447};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01532, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2283027,
CC ECO:0000269|PubMed:8262918}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01532, ECO:0000269|PubMed:8262918}.
CC -!- INDUCTION: Induced by L-rhamnose via the RhaR-RhaS regulatory cascade
CC (PubMed:8757746). Also induced by L-mannose or L-lyxose
CC (PubMed:1650346, PubMed:8757746). {ECO:0000269|PubMed:1650346,
CC ECO:0000269|PubMed:8757746}.
CC -!- SIMILARITY: Belongs to the L-rhamnose transporter (TC 2.A.7.6) family.
CC {ECO:0000255|HAMAP-Rule:MF_01532, ECO:0000305}.
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DR EMBL; M85158; AAA24529.1; -; Genomic_DNA.
DR EMBL; X60699; CAA43109.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03040.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76889.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77402.1; -; Genomic_DNA.
DR PIR; B42436; B42436.
DR RefSeq; NP_418343.1; NC_000913.3.
DR RefSeq; WP_000063526.1; NZ_LN832404.1.
DR AlphaFoldDB; P27125; -.
DR BioGRID; 4263535; 4.
DR STRING; 511145.b3907; -.
DR TCDB; 2.A.7.6.1; the drug/metabolite transporter (dmt) superfamily.
DR PaxDb; P27125; -.
DR PRIDE; P27125; -.
DR EnsemblBacteria; AAC76889; AAC76889; b3907.
DR EnsemblBacteria; BAE77402; BAE77402; BAE77402.
DR GeneID; 948398; -.
DR KEGG; ecj:JW3878; -.
DR KEGG; eco:b3907; -.
DR PATRIC; fig|1411691.4.peg.2798; -.
DR EchoBASE; EB1289; -.
DR eggNOG; ENOG502Z7ID; Bacteria.
DR HOGENOM; CLU_066437_0_0_6; -.
DR InParanoid; P27125; -.
DR OMA; QFFFYGM; -.
DR PhylomeDB; P27125; -.
DR BioCyc; EcoCyc:RHAT-MON; -.
DR BioCyc; MetaCyc:RHAT-MON; -.
DR PRO; PR:P27125; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015153; F:rhamnose transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015293; F:symporter activity; IDA:EcoCyc.
DR GO; GO:0015762; P:rhamnose transmembrane transport; IMP:EcoCyc.
DR HAMAP; MF_01532; RhaT; 1.
DR InterPro; IPR004673; L-rhamnose-proton_sym_RhaT.
DR Pfam; PF06379; RhaT; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..344
FT /note="L-rhamnose-proton symporter"
FT /id="PRO_0000208272"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..73
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..136
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..213
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..289
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8262918"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 344 AA; 37320 MW; F73C3CC9CBEA3C28 CRC64;
MSNAITMGIF WHLIGAASAA CFYAPFKKVK KWSWETMWSV GGIVSWIILP WAISALLLPN
FWAYYSSFSL STRLPVFLFG AMWGIGNINY GLTMRYLGMS MGIGIAIGIT LIVGTLMTPI
INGNFDVLIS TEGGRMTLLG VLVALIGVGI VTRAGQLKER KMGIKAEEFN LKKGLVLAVM
CGIFSAGMSF AMNAAKPMHE AAAALGVDPL YVALPSYVVI MGGGAIINLG FCFIRLAKVK
DLSLKADFSL AKSLIIHNVL LSTLGGLMWY LQFFFYAWGH ARIPAQYDYI SWMLHMSFYV
LCGGIVGLVL KEWNNAGRRP VTVLSLGCVV IIVAANIVGI GMAN
