MHPT_ECOLI
ID MHPT_ECOLI Reviewed; 403 AA.
AC P77589; P77037; Q2MC71;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=3-(3-hydroxy-phenyl)propionate transporter;
DE Short=3HPP transporter;
DE AltName: Full=3-(3-hydroxy-phenyl)propionate:H(+) symporter;
DE Short=3HPP:H(+) symporter;
GN Name=mhpT; Synonyms=yaiK; OrderedLocusNames=b0353, JW5046;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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 83-330, AND PROBABLE FUNCTION.
RC STRAIN=K12 / CS520;
RX PubMed=9098055; DOI=10.1128/jb.179.8.2573-2581.1997;
RA Ferrandez A., Garcia J.L., Diaz E.;
RT "Genetic characterization and expression in heterologous hosts of the 3-(3-
RT hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12.";
RL J. Bacteriol. 179:2573-2581(1997).
RN [6]
RP 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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-27; ASP-75; ALA-272 AND LYS-276.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=23934492; DOI=10.1128/aem.02110-13;
RA Xu Y., Chen B., Chao H., Zhou N.Y.;
RT "mhpT encodes an active transporter involved in 3-(3-
RT hydroxyphenyl)propionate catabolism by Escherichia coli K-12.";
RL Appl. Environ. Microbiol. 79:6362-6368(2013).
CC -!- FUNCTION: Uptake of 3-(3-hydroxyphenyl)propionate (3HPP) across the
CC cytoplasmic membrane. Transport is driven by the proton motive force.
CC Does not transport benzoate, 3-hydroxybenzoate or gentisate.
CC {ECO:0000269|PubMed:23934492}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:23934492}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23934492}.
CC -!- INDUCTION: Induced by 3HPP. {ECO:0000269|PubMed:23934492}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant loses the ability to utilize 3HPP
CC at pH 8.2. {ECO:0000269|PubMed:23934492}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Aromatic
CC acid:H(+) symporter (AAHS) (TC 2.A.1.15) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18077.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=D85613; Type=Frameshift; Evidence={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; D85613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U73857; AAB18077.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73456.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76135.1; -; Genomic_DNA.
DR EMBL; X97543; CAA66145.1; -; Genomic_DNA.
DR PIR; A64763; A64763.
DR RefSeq; NP_414887.2; NC_000913.3.
DR RefSeq; WP_000107627.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P77589; -.
DR SMR; P77589; -.
DR BioGRID; 4261625; 23.
DR STRING; 511145.b0353; -.
DR TCDB; 2.A.1.15.2; the major facilitator superfamily (mfs).
DR PaxDb; P77589; -.
DR PRIDE; P77589; -.
DR EnsemblBacteria; AAC73456; AAC73456; b0353.
DR EnsemblBacteria; BAE76135; BAE76135; BAE76135.
DR GeneID; 944997; -.
DR KEGG; ecj:JW5046; -.
DR KEGG; eco:b0353; -.
DR PATRIC; fig|1411691.4.peg.1925; -.
DR EchoBASE; EB3078; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_46_4_6; -.
DR InParanoid; P77589; -.
DR OMA; LINWLPM; -.
DR PhylomeDB; P77589; -.
DR BioCyc; EcoCyc:MHPT-MON; -.
DR BioCyc; MetaCyc:MHPT-MON; -.
DR PRO; PR:P77589; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 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..403
FT /note="3-(3-hydroxy-phenyl)propionate transporter"
FT /id="PRO_0000050308"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..105
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..253
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..306
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..369
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 27
FT /note="E->A: Lack of 3HPP transport activity."
FT /evidence="ECO:0000269|PubMed:23934492"
FT MUTAGEN 27
FT /note="E->D: Slight decrease in 3HPP transport activity."
FT /evidence="ECO:0000269|PubMed:23934492"
FT MUTAGEN 75
FT /note="D->A,E: Lack of 3HPP transport activity."
FT /evidence="ECO:0000269|PubMed:23934492"
FT MUTAGEN 272
FT /note="A->H: 30% increase in 3HPP transport activity."
FT /evidence="ECO:0000269|PubMed:23934492"
FT MUTAGEN 276
FT /note="K->D: Lack of 3HPP transport activity."
FT /evidence="ECO:0000269|PubMed:23934492"
FT CONFLICT 295
FT /note="L -> V (in Ref. 5; D85613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 41551 MW; 85EE921E57686FEB CRC64;
MSTRTPSSSS SRLMLTIGLC FLVALMEGLD LQAAGIAAGG IAQAFALDKM QMGWIFSAGI
LGLLPGALVG GMLADRYGRK RILIGSVALF GLFSLATAIA WDFPSLVFAR LMTGVGLGAA
LPNLIALTSE AAGPRFRGTA VSLMYCGVPI GAALAATLGF AGANLAWQTV FWVGGVVPLI
LVPLLMRWLP ESAVFAGEKQ SAPPLRALFA PETATATLLL WLCYFFTLLV VYMLINWLPL
LLVEQGFQPS QAAGVMFALQ MGAASGTLML GALMDKLRPV TMSLLIYSGM LASLLALGTV
SSFNGMLLAG FVAGLFATGG QSVLYALAPL FYSSQIRATG VGTAVAVGRL GAMSGPLLAG
KMLALGTGTV GVMAASAPGI LVAGLAVFIL MSRRSRIQPC ADA
