FUCP_ECOLI
ID FUCP_ECOLI Reviewed; 438 AA.
AC P11551; Q2MA33;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=L-fucose-proton symporter {ECO:0000305};
DE AltName: Full=6-deoxy-L-galactose permease;
DE AltName: Full=L-fucose permease;
DE AltName: Full=L-fucose-H(+) symport protein {ECO:0000303|PubMed:7783647};
GN Name=fucP; OrderedLocusNames=b2801, JW2772;
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;
RX PubMed=2664711; DOI=10.1093/nar/17.12.4883;
RA Lu Z., Lin E.C.C.;
RT "The nucleotide sequence of Escherichia coli genes for L-fucose
RT dissimilation.";
RL Nucleic Acids Res. 17:4883-4884(1989).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=2553671; DOI=10.1128/jb.171.11.6097-6105.1989;
RA Chen Y.M., Lu Z., Lin E.C.C.;
RT "Constitutive activation of the fucAO operon and silencing of the
RT divergently transcribed fucPIK operon by an IS5 element in Escherichia coli
RT mutants selected for growth on L-1,2-propanediol.";
RL J. Bacteriol. 171:6097-6105(1989).
RN [5]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8052131; DOI=10.1111/j.1365-2958.1994.tb01066.x;
RA Gunn F.J., Tate C.G., Henderson P.J.F.;
RT "Identification of a novel sugar-H+ symport protein, FucP, for transport of
RT L-fucose into Escherichia coli.";
RL Mol. Microbiol. 12:799-809(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=JM2418;
RX PubMed=2829831; DOI=10.1042/bj2480495;
RA Bradley S.A., Tinsley C.R., Muiry J.A., Henderson P.J.F.;
RT "Proton-linked L-fucose transport in Escherichia coli.";
RL Biochem. J. 248:495-500(1987).
RN [7]
RP TOPOLOGY.
RX PubMed=7783647; DOI=10.1111/j.1365-2958.1995.tb02384.x;
RA Gunn F.J., Tate C.G., Sansom C.E., Henderson P.J.F.;
RT "Topological analyses of the L-fucose-H+ symport protein, FucP, from
RT Escherichia coli.";
RL Mol. Microbiol. 15:771-783(1995).
RN [8]
RP FUNCTION, AND SUBSTRATE-BINDING.
RX PubMed=9826601; DOI=10.1016/s0006-3495(98)77722-7;
RA Spooner P.J., O'Reilly W.J., Homans S.W., Rutherford N.G., Henderson P.J.,
RA Watts A.;
RT "Weak substrate binding to transport proteins studied by NMR.";
RL Biophys. J. 75:2794-2800(1998).
RN [9]
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).
RN [10]
RP CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF TRP-38 AND TRP-278.
RX PubMed=22930818; DOI=10.1073/pnas.1213445109;
RA Sugihara J., Sun L., Yan N., Kaback H.R.;
RT "Dynamics of the L-fucose/H+ symporter revealed by fluorescence
RT spectroscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14847-14851(2012).
RN [11] {ECO:0007744|PDB:3O7P, ECO:0007744|PDB:3O7Q}
RP X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF WILD-TYPE AND OF MUTANT ALA-162,
RP SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF ASP-46 AND
RP GLU-135.
RX PubMed=20877283; DOI=10.1038/nature09406;
RA Dang S., Sun L., Huang Y., Lu F., Liu Y., Gong H., Wang J., Yan N.;
RT "Structure of a fucose transporter in an outward-open conformation.";
RL Nature 467:734-738(2010).
CC -!- FUNCTION: Mediates the uptake of L-fucose across the boundary membrane
CC with the concomitant transport of protons into the cell (symport
CC system) (PubMed:2829831, PubMed:8052131). Can also transport L-
CC galactose and D-arabinose, but at reduced rates compared with L-fucose.
CC Is not able to transport L-rhamnose and L-arabinose (PubMed:2829831).
CC Binds D-arabinose with the highest affinity, followed by L-fucose, and
CC then by L-galactose (PubMed:9826601). {ECO:0000269|PubMed:2829831,
CC ECO:0000269|PubMed:8052131, ECO:0000269|PubMed:9826601}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-fucose(in) = H(+)(out) + L-fucose(out);
CC Xref=Rhea:RHEA:29023, ChEBI:CHEBI:2181, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:22930818, ECO:0000269|PubMed:2829831,
CC ECO:0000269|PubMed:8052131};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29025;
CC Evidence={ECO:0000269|PubMed:2829831, ECO:0000269|PubMed:8052131};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose(out) + H(+)(out) = D-arabinose(in) + H(+)(in);
CC Xref=Rhea:RHEA:66428, ChEBI:CHEBI:15378, ChEBI:CHEBI:46994;
CC Evidence={ECO:0000269|PubMed:2829831};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-galactose(out) = H(+)(in) + L-galactose(in);
CC Xref=Rhea:RHEA:66432, ChEBI:CHEBI:15378, ChEBI:CHEBI:37619;
CC Evidence={ECO:0000269|PubMed:2829831};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 for fucose transport. {ECO:0000269|PubMed:2829831};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:20877283}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20877283}.
CC -!- INDUCTION: By L-fucose. {ECO:0000269|PubMed:2829831}.
CC -!- DOMAIN: Contains an outward-open, amphipathic cavity. Contains only two
CC acidic residues along the transport path, Asp-46 and Glu-135, which can
CC undergo cycles of protonation and deprotonation. Asp-46 and Glu-135
CC have an essential role, coupling proton translocation and substrate
CC recognition (PubMed:20877283). Sugar binding probably induces a
CC conformational change in which the outward-facing cavity closes,
CC thereby bringing Trp-38 and Trp-278 into close proximity around the
CC bound sugar to form an occluded intermediate (PubMed:22930818).
CC {ECO:0000269|PubMed:20877283, ECO:0000269|PubMed:22930818}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. FHS
CC transporter (TC 2.A.1.7) family. {ECO:0000305}.
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DR EMBL; X15025; CAA33126.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40451.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75843.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76873.1; -; Genomic_DNA.
DR EMBL; M31059; AAA23822.2; -; Genomic_DNA.
DR PIR; JS0184; WQECFP.
DR RefSeq; NP_417281.1; NC_000913.3.
DR RefSeq; WP_000528603.1; NZ_STEB01000030.1.
DR PDB; 3O7P; X-ray; 3.20 A; A=1-438.
DR PDB; 3O7Q; X-ray; 3.14 A; A=1-438.
DR PDBsum; 3O7P; -.
DR PDBsum; 3O7Q; -.
DR AlphaFoldDB; P11551; -.
DR BMRB; P11551; -.
DR SMR; P11551; -.
DR BioGRID; 4260704; 18.
DR STRING; 511145.b2801; -.
DR TCDB; 2.A.1.7.1; the major facilitator superfamily (mfs).
DR PaxDb; P11551; -.
DR PRIDE; P11551; -.
DR EnsemblBacteria; AAC75843; AAC75843; b2801.
DR EnsemblBacteria; BAE76873; BAE76873; BAE76873.
DR GeneID; 66673332; -.
DR GeneID; 947487; -.
DR KEGG; ecj:JW2772; -.
DR KEGG; eco:b2801; -.
DR PATRIC; fig|1411691.4.peg.3932; -.
DR EchoBASE; EB0348; -.
DR eggNOG; COG0738; Bacteria.
DR HOGENOM; CLU_028452_0_1_6; -.
DR InParanoid; P11551; -.
DR OMA; TGMSMLY; -.
DR PhylomeDB; P11551; -.
DR BioCyc; EcoCyc:FUCP-MON; -.
DR BioCyc; MetaCyc:FUCP-MON; -.
DR EvolutionaryTrace; P11551; -.
DR PRO; PR:P11551; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015518; F:arabinose:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015535; F:fucose:proton symporter activity; IMP:EcoCyc.
DR GO; GO:0015517; F:galactose:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015751; P:arabinose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015756; P:fucose transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015757; P:galactose transmembrane transport; IDA:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR005275; Lfuc_symporter_FucP.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00885; fucP; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Fucose metabolism; Membrane; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8052131"
FT CHAIN 2..438
FT /note="L-fucose-proton symporter"
FT /id="PRO_0000094501"
FT TOPO_DOM 2..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 27..53
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 54..61
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 62..87
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 88..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 114..117
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 118..144
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 145..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 151..178
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 179..193
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 194..227
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 228..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 258..287
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 288..293
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 294..319
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 320..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 325..343
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 344..347
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 348..372
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 373..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 380..407
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 408..410
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TRANSMEM 411..430
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20877283"
FT TOPO_DOM 431..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:20877283"
FT SITE 46
FT /note="Important for activity"
FT /evidence="ECO:0000269|PubMed:20877283"
FT SITE 135
FT /note="Important for activity"
FT /evidence="ECO:0000269|PubMed:20877283"
FT MUTAGEN 38
FT /note="W->F,I,Y: Strong decrease in L-fucose transport."
FT /evidence="ECO:0000269|PubMed:22930818"
FT MUTAGEN 46
FT /note="D->A,N: Loss of L-fucose transport."
FT /evidence="ECO:0000269|PubMed:20877283"
FT MUTAGEN 135
FT /note="E->A,D,Q: Loss of L-fucose transport."
FT /evidence="ECO:0000269|PubMed:20877283"
FT MUTAGEN 278
FT /note="W->F,Y: Slight decrease in L-fucose transport."
FT /evidence="ECO:0000269|PubMed:22930818"
FT MUTAGEN 278
FT /note="W->I: 30% decrease in L-fucose transport."
FT /evidence="ECO:0000269|PubMed:22930818"
FT HELIX 25..55
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 90..113
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 117..144
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3O7P"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 194..228
FT /evidence="ECO:0007829|PDB:3O7Q"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3O7P"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 259..288
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 294..321
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 324..344
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 380..389
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 392..408
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:3O7Q"
FT HELIX 416..429
FT /evidence="ECO:0007829|PDB:3O7Q"
SQ SEQUENCE 438 AA; 47545 MW; D8AA3785274A0085 CRC64;
MGNTSIQTQS YRAVDKDAGQ SRSYIIPFAL LCSLFFLWAV ANNLNDILLP QFQQAFTLTN
FQAGLIQSAF YFGYFIIPIP AGILMKKLSY KAGIITGLFL YALGAALFWP AAEIMNYTLF
LVGLFIIAAG LGCLETAANP FVTVLGPESS GHFRLNLAQT FNSFGAIIAV VFGQSLILSN
VPHQSQDVLD KMSPEQLSAY KHSLVLSVQT PYMIIVAIVL LVALLIMLTK FPALQSDNHS
DAKQGSFSAS LSRLARIRHW RWAVLAQFCY VGAQTACWSY LIRYAVEEIP GMTAGFAANY
LTGTMVCFFI GRFTGTWLIS RFAPHKVLAA YALIAMALCL ISAFAGGHVG LIALTLCSAF
MSIQYPTIFS LGIKNLGQDT KYGSSFIVMT IIGGGIVTPV MGFVSDAAGN IPTAELIPAL
CFAVIFIFAR FRSQTATN
