YTFQ_ECOLI
ID YTFQ_ECOLI Reviewed; 318 AA.
AC P39325; Q2M678;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Galactofuranose-binding protein YtfQ {ECO:0000305};
DE Flags: Precursor;
GN Name=ytfQ; OrderedLocusNames=b4227, JW4186;
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 PROTEIN SEQUENCE OF 22-33.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5] {ECO:0007744|PDB:2VK2}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 22-318 IN COMPLEX WITH
RP BETA-D-GALACTOFURANOSE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISULFIDE BOND.
RC STRAIN=K12;
RX PubMed=19744923; DOI=10.1074/jbc.m109.054296;
RA Horler R.S., Muller A., Williamson D.C., Potts J.R., Wilson K.S.,
RA Thomas G.H.;
RT "Furanose-specific sugar transport: characterization of a bacterial
RT galactofuranose-binding protein.";
RL J. Biol. Chem. 284:31156-31163(2009).
CC -!- FUNCTION: Part of the ABC transporter complex YtfQRT-YjfF involved in
CC galactofuranose transport (Probable). Binds to both alpha- and beta-
CC galactofuranose (PubMed:19744923). {ECO:0000269|PubMed:19744923,
CC ECO:0000305|PubMed:19744923}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (YtfR),
CC two transmembrane proteins (YtfT and YjfF) and a solute-binding protein
CC (YtfQ). {ECO:0000305|PubMed:19744923}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:19744923}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; U14003; AAA97124.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77184.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78228.1; -; Genomic_DNA.
DR PIR; S56453; S56453.
DR RefSeq; NP_418648.1; NC_000913.3.
DR RefSeq; WP_000265913.1; NZ_LN832404.1.
DR PDB; 2VK2; X-ray; 1.20 A; A=22-318.
DR PDBsum; 2VK2; -.
DR AlphaFoldDB; P39325; -.
DR SMR; P39325; -.
DR BioGRID; 4259313; 8.
DR BioGRID; 853035; 6.
DR ComplexPortal; CPX-4323; Galactofuranose ABC transporter complex.
DR IntAct; P39325; 8.
DR STRING; 511145.b4227; -.
DR TCDB; 3.A.1.2.25; the atp-binding cassette (abc) superfamily.
DR jPOST; P39325; -.
DR PaxDb; P39325; -.
DR PRIDE; P39325; -.
DR EnsemblBacteria; AAC77184; AAC77184; b4227.
DR EnsemblBacteria; BAE78228; BAE78228; BAE78228.
DR GeneID; 948746; -.
DR KEGG; ecj:JW4186; -.
DR KEGG; eco:b4227; -.
DR PATRIC; fig|1411691.4.peg.2474; -.
DR EchoBASE; EB2409; -.
DR eggNOG; COG1879; Bacteria.
DR HOGENOM; CLU_037628_3_2_6; -.
DR InParanoid; P39325; -.
DR OMA; EWRTANT; -.
DR PhylomeDB; P39325; -.
DR BioCyc; EcoCyc:YTFQ-MON; -.
DR BioCyc; MetaCyc:YTFQ-MON; -.
DR BRENDA; 7.5.2.9; 2026.
DR EvolutionaryTrace; P39325; -.
DR PRO; PR:P39325; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005534; F:galactose binding; IDA:EcoCyc.
DR GO; GO:0015757; P:galactose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0140271; P:hexose import across plasma membrane; IC:ComplexPortal.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm;
KW Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 22..318
FT /note="Galactofuranose-binding protein YtfQ"
FT /id="PRO_0000031745"
FT BINDING 34..38
FT /ligand="beta-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:59497"
FT /evidence="ECO:0000269|PubMed:19744923,
FT ECO:0007744|PDB:2VK2"
FT BINDING 111..112
FT /ligand="beta-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:59497"
FT /evidence="ECO:0000269|PubMed:19744923,
FT ECO:0007744|PDB:2VK2"
FT BINDING 167
FT /ligand="beta-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:59497"
FT /evidence="ECO:0000269|PubMed:19744923,
FT ECO:0007744|PDB:2VK2"
FT BINDING 220
FT /ligand="beta-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:59497"
FT /evidence="ECO:0000269|PubMed:19744923,
FT ECO:0007744|PDB:2VK2"
FT BINDING 248
FT /ligand="beta-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:59497"
FT /evidence="ECO:0000269|PubMed:19744923,
FT ECO:0007744|PDB:2VK2"
FT DISULFID 150..214
FT /evidence="ECO:0000269|PubMed:19744923"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:2VK2"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:2VK2"
FT TURN 208..212
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:2VK2"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:2VK2"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:2VK2"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:2VK2"
SQ SEQUENCE 318 AA; 34345 MW; 5FF0724EA4717F95 CRC64;
MWKRLLIVSA VSAAMSSMAL AAPLTVGFSQ VGSESGWRAA ETNVAKSEAE KRGITLKIAD
GQQKQENQIK AVRSFVAQGV DAIFIAPVVA TGWEPVLKEA KDAEIPVFLL DRSIDVKDKS
LYMTTVTADN ILEGKLIGDW LVKEVNGKPC NVVELQGTVG ASVAIDRKKG FAEAIKNAPN
IKIIRSQSGD FTRSKGKEVM ESFIKAENNG KNICMVYAHN DDMVIGAIQA IKEAGLKPGK
DILTGSIDGV PDIYKAMMDG EANASVELTP NMAGPAFDAL EKYKKDGTMP EKLTLTKSTL
YLPDTAKEEL EKKKNMGY
