ID   MDXE_BACSU              Reviewed;         417 AA.
AC   O06989; Q795G8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Maltodextrin-binding protein MdxE;
DE   Flags: Precursor;
GN   Name=mdxE; Synonyms=yvdG; OrderedLocusNames=BSU34610;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Denizot F.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION AS A MALTODEXTRIN-BINDING PROTEIN, INDUCTION, ACTIVITY REGULATION,
RP   AND GENE NAME.
RC   STRAIN=168;
RX   PubMed=16707683; DOI=10.1128/jb.00213-06;
RA   Schoenert S., Seitz S., Krafft H., Feuerbaum E.-A., Andernach I., Witz G.,
RA   Dahl M.K.;
RT   "Maltose and maltodextrin utilization by Bacillus subtilis.";
RL   J. Bacteriol. 188:3911-3922(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex involved in maltodextrin
CC       import. Binds maltodextrin. Can also bind maltose with low affinity,
CC       but is not involved in its uptake. {ECO:0000269|PubMed:16707683}.
CC   -!- ACTIVITY REGULATION: Inhibited by glucose and lactose.
CC       {ECO:0000269|PubMed:16707683}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmX),
CC       two transmembrane proteins (MdxF and MdxG) and a solute-binding protein
CC       (MdxE). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: Induced by maltose and repressed by glucose.
CC       {ECO:0000269|PubMed:16707683}.
CC   -!- MISCELLANEOUS: Maltodextrin can also be transported inside the cell
CC       after degradation to maltose by extracellular amylase AmyE, transported
CC       as maltose by MalP.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z94043; CAB08036.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15466.1; -; Genomic_DNA.
DR   PIR; G70033; G70033.
DR   RefSeq; NP_391341.1; NC_000964.3.
DR   RefSeq; WP_003243721.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O06989; -.
DR   SMR; O06989; -.
DR   STRING; 224308.BSU34610; -.
DR   TCDB; 3.A.1.1.26; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O06989; -.
DR   PRIDE; O06989; -.
DR   EnsemblBacteria; CAB15466; CAB15466; BSU_34610.
DR   GeneID; 936522; -.
DR   KEGG; bsu:BSU34610; -.
DR   PATRIC; fig|224308.179.peg.3748; -.
DR   eggNOG; COG2182; Bacteria.
DR   InParanoid; O06989; -.
DR   OMA; WAHDWIG; -.
DR   PhylomeDB; O06989; -.
DR   BioCyc; BSUB:BSU34610-MON; -.
DR   SABIO-RK; O06989; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR   GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1901982; F:maltose binding; IBA:GO_Central.
DR   GO; GO:0042956; P:maltodextrin transmembrane transport; IBA:GO_Central.
DR   GO; GO:0015768; P:maltose transport; IBA:GO_Central.
DR   InterPro; IPR006060; Maltose/Cyclodextrin-bd.
DR   InterPro; IPR006059; SBP.
DR   Pfam; PF13416; SBP_bac_8; 1.
DR   PRINTS; PR00181; MALTOSEBP.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Polysaccharide transport;
KW   Reference proteome; Signal; Sugar transport; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..417
FT                   /note="Maltodextrin-binding protein MdxE"
FT                   /id="PRO_0000360702"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   417 AA;  45601 MW;  31A27A4CA724BA5D CRC64;
     MVLLKKGFAI LAASFLAIGL AACSSSKNPA SSDGKKVLTV SVEETYKEYI ESIKTKFEKE
     NDVTVKIVEK QMFEQLEALP LDGPAGNAPD VMLAAYDRIG GLGQQGHLLD IKPSNTKSFG
     DKEMQQVTVD GKVYGMPLVI ETLILYYNKD LLKTAPKTFK DLEKLTEDPR FAFASEKGKS
     TGFLAKWTDF YMSYGLLAGY GGYVFGKNGT DSGDIGLNNK GAVEAVKYAE KWFETYWPKG
     MQDNSSADDF IQQMFLEGKA AAIIGGPWSA ANYKEAKLNY GAAPIPTLPN GEEYAPFAGG
     KGWVASKYTK EPELAEKWLE YAANDANAYA FYEDTNEVPA NTAARKKADE QKNELTSAVI
     KQYETATPTP NIPEMAEVWT GAESLIFDAA SGKKSTQTSA NDAVNVIKEN IKEKYVK