MALE_ECO57
ID MALE_ECO57 Reviewed; 396 AA.
AC P0AEY0; P02928;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Maltose/maltodextrin-binding periplasmic protein {ECO:0000250|UniProtKB:P0AEX9};
DE AltName: Full=MMBP {ECO:0000250|UniProtKB:P0AEX9};
DE AltName: Full=Maltodextrin-binding protein {ECO:0000250|UniProtKB:P0AEX9};
DE AltName: Full=Maltose-binding protein {ECO:0000250|UniProtKB:P0AEX9};
DE Short=MBP {ECO:0000250|UniProtKB:P0AEX9};
DE Flags: Precursor;
GN Name=malE; OrderedLocusNames=Z5632, ECs5017;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC maltose/maltodextrin import. Binds maltose and higher maltodextrins.
CC {ECO:0000250|UniProtKB:P0AEX9}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MalK),
CC two transmembrane proteins (MalG and MalF) and a solute-binding protein
CC (MalE). {ECO:0000250|UniProtKB:P0AEX9}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0AEX9}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG59233.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38440.1; -; Genomic_DNA.
DR PIR; A98256; A98256.
DR PIR; E86096; E86096.
DR RefSeq; NP_313044.1; NC_002695.1.
DR RefSeq; WP_000695387.1; NZ_SWKA01000005.1.
DR PDB; 3VD8; X-ray; 2.07 A; A=27-384.
DR PDB; 4MY2; X-ray; 2.40 A; A=26-392.
DR PDB; 4WGI; X-ray; 1.85 A; A=27-392.
DR PDB; 4WVG; X-ray; 2.05 A; A=33-392.
DR PDB; 4WVI; X-ray; 1.90 A; A=33-392.
DR PDB; 4WVJ; X-ray; 1.95 A; A=33-392.
DR PDB; 4XAI; X-ray; 2.60 A; A/B=27-392.
DR PDB; 4XAJ; X-ray; 3.55 A; A/B/C/D=26-392.
DR PDB; 4YS9; X-ray; 2.00 A; B=27-392.
DR PDB; 5CL1; X-ray; 3.80 A; A/B=26-392.
DR PDB; 5E7U; X-ray; 2.80 A; A=27-392.
DR PDB; 5JON; X-ray; 2.04 A; A/B=27-392.
DR PDB; 5LOF; X-ray; 2.20 A; A=27-392.
DR PDBsum; 3VD8; -.
DR PDBsum; 4MY2; -.
DR PDBsum; 4WGI; -.
DR PDBsum; 4WVG; -.
DR PDBsum; 4WVI; -.
DR PDBsum; 4WVJ; -.
DR PDBsum; 4XAI; -.
DR PDBsum; 4XAJ; -.
DR PDBsum; 4YS9; -.
DR PDBsum; 5CL1; -.
DR PDBsum; 5E7U; -.
DR PDBsum; 5JON; -.
DR PDBsum; 5LOF; -.
DR AlphaFoldDB; P0AEY0; -.
DR BMRB; P0AEY0; -.
DR SMR; P0AEY0; -.
DR IntAct; P0AEY0; 1.
DR MINT; P0AEY0; -.
DR STRING; 155864.EDL933_5371; -.
DR ABCD; P0AEY0; 7 sequenced antibodies.
DR EnsemblBacteria; AAG59233; AAG59233; Z5632.
DR EnsemblBacteria; BAB38440; BAB38440; ECs_5017.
DR GeneID; 66672051; -.
DR GeneID; 914317; -.
DR KEGG; ece:Z5632; -.
DR KEGG; ecs:ECs_5017; -.
DR PATRIC; fig|386585.9.peg.5240; -.
DR eggNOG; COG2182; Bacteria.
DR HOGENOM; CLU_031285_17_0_6; -.
DR OMA; WAHDWIG; -.
DR BRENDA; 3.5.4.38; 12088.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR006060; Maltose/Cyclodextrin-bd.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR Pfam; PF01547; SBP_bac_1; 1.
DR PRINTS; PR00181; MALTOSEBP.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Reference proteome; Signal; Sugar transport;
KW Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..396
FT /note="Maltose/maltodextrin-binding periplasmic protein"
FT /id="PRO_0000044622"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:4WGI"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4WGI"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:4WGI"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:4WGI"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:4XAI"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 341..352
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4WGI"
FT HELIX 362..377
FT /evidence="ECO:0007829|PDB:4WGI"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4WVJ"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:4WGI"
SQ SEQUENCE 396 AA; 43388 MW; A4C1B3C1777ADE47 CRC64;
MKIKTGARIL ALSALTTMMF SASALAKIEE GKLVIWINGD KGYNGLAEVG KKFEKDTGIK
VTVEHPDKLE EKFPQVAATG DGPDIIFWAH DRFGGYAQSG LLAEITPDKA FQDKLYPFTW
DAVRYNGKLI AYPIAVEALS LIYNKDLLPN PPKTWEEIPA LDKELKAKGK SALMFNLQEP
YFTWPLIAAD GGYAFKYENG KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE
AAFNKGETAM TINGPWAWSN IDTSKVNYGV TVLPTFKGQP SKPFVGVLSA GINAASPNKE
LAKEFLENYL LTDEGLEAVN KDKPLGAVAL KSYEEELAKD PRIAATMENA QKGEIMPNIP
QMSAFWYAVR TAVINAASGR QTVDEALKDA QTRITK
