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MDXF_BACSU
ID   MDXF_BACSU              Reviewed;         435 AA.
AC   O06990; Q795G9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Maltodextrin transport system permease protein MdxF;
GN   Name=mdxF; Synonyms=yvdH; OrderedLocusNames=BSU34600;
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, AND NOMENCLATURE.
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. Probably responsible for the translocation of the substrate
CC       across the membrane (Probable). {ECO:0000305|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:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. MalFG subfamily. {ECO:0000305}.
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DR   EMBL; Z94043; CAB08037.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15465.1; -; Genomic_DNA.
DR   PIR; H70033; H70033.
DR   RefSeq; NP_391340.1; NC_000964.3.
DR   RefSeq; WP_003243114.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O06990; -.
DR   SMR; O06990; -.
DR   STRING; 224308.BSU34600; -.
DR   TCDB; 3.A.1.1.26; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O06990; -.
DR   PRIDE; O06990; -.
DR   EnsemblBacteria; CAB15465; CAB15465; BSU_34600.
DR   GeneID; 937063; -.
DR   KEGG; bsu:BSU34600; -.
DR   PATRIC; fig|224308.179.peg.3747; -.
DR   eggNOG; COG1175; Bacteria.
DR   InParanoid; O06990; -.
DR   OMA; WYAYAMI; -.
DR   PhylomeDB; O06990; -.
DR   BioCyc; BSUB:BSU34600-MON; -.
DR   SABIO-RK; O06990; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:1990060; C:maltose transport complex; IBA:GO_Central.
DR   GO; GO:0015423; F:ABC-type maltose transporter activity; IBA:GO_Central.
DR   GO; GO:0042956; P:maltodextrin transmembrane transport; IBA:GO_Central.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR030156; MalF-like.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   PANTHER; PTHR47314:SF1; PTHR47314:SF1; 2.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Polysaccharide transport; Reference proteome;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..435
FT                   /note="Maltodextrin transport system permease protein MdxF"
FT                   /id="PRO_0000361678"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        403..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          195..422
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   435 AA;  48529 MW;  31E86E8B0E7797DC CRC64;
     MNKHHTLTKQ KRKAGLLSII PGLGQIANQQ LSKGLLFLAI TGLFAFELCV FGIQALTGLM
     TLGSVPGEDH SLFMLIEGTL QLIVTMIFLM FYIFNIHDSR KTAAMKAAGL EVNTTAKDMI
     CHAGDKGFPY LFTLPAYIMM VFVIIFPVLV TLFVALTNYD FYHIPPNRLI DWVGFKNFLN
     IFFLGSYRET FVNVLGWTVI WTICATTLQI ILGIVTALFV NQDFIKGKRI FRMIFLFPWA
     VPAFITIMSF SNMFNDSIGA VNAQVIPLFN HLPFVELPAI AWKTDPFWTK TALIMIQTWL
     GFPYIYVMVT GVLQAIPGEL YEAAKIDGAT FIQRFRHITF PMILFATAPV MITQYTFNFN
     NFSIIYLFNE GGPGSAGAGA GSTDILISWI YKLTTGTSPQ YSVAAAVTLL ISFIVIGISL
     IAFKKSNAFG NEEVM
 
 
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