ID   MALF_VIBVY              Reviewed;         523 AA.
AC   Q7MFC2;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN   Name=malF; OrderedLocusNames=VVA0398;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC       maltose/maltodextrin import. Probably responsible for the translocation
CC       of the substrate across the membrane. {ECO:0000250|UniProtKB:P02916}.
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:P02916}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P02916}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P02916}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. MalFG subfamily. {ECO:0000305}.
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DR   EMBL; BA000038; BAC96424.1; -; Genomic_DNA.
DR   RefSeq; WP_011082432.1; NC_005140.1.
DR   AlphaFoldDB; Q7MFC2; -.
DR   SMR; Q7MFC2; -.
DR   STRING; 672.VV93_v1c33850; -.
DR   EnsemblBacteria; BAC96424; BAC96424; BAC96424.
DR   GeneID; 66966940; -.
DR   KEGG; vvy:VVA0398; -.
DR   eggNOG; COG1175; Bacteria.
DR   HOGENOM; CLU_016047_20_0_6; -.
DR   OMA; DGHNSTK; -.
DR   OrthoDB; 1619224at2; -.
DR   Proteomes; UP000002675; Chromosome II.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   Gene3D; 1.20.58.370; -; 1.
DR   InterPro; IPR030156; MalF-like.
DR   InterPro; IPR035277; MalF_N.
DR   InterPro; IPR029345; MalF_P2.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   PANTHER; PTHR47314:SF1; PTHR47314:SF1; 1.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF14785; MalF_P2; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..523
FT                   /note="Maltose/maltodextrin transport system permease
FT                   protein MalF"
FT                   /id="PRO_0000060079"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        46..49
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        70..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        105..288
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        312..322
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        346..378
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        402..434
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        435..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        458..492
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        516..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          290..514
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   523 AA;  57107 MW;  6F2200184A02B77C CRC64;
     MQSVQGTDAM TAPAASLPGS KKVFIKWALL GTVGLINGYA TILMYSRGEV AFAMLTVILT
     ALALYVFGSK KTYAHRYIYP GIAGMILFIL FPLAYTVGLA FTNYSAKNQL SLDRAQSVLL
     DRTFQSGESY PFTLYKTDSG HRIVIKDGDV LLSTPEFVLG SAISDLDLSP VDTVSGTAEP
     IKTIVSNRTA LSSIDLHFAN GDDIRMSGLR KFAGVVPLYT MQADGETLKN NQTGELLKPN
     MDVGFYQAMD EAGNFVGNTV SPGFVVQIGT DNFERVWKDD GIKEPFISIF IWTVVFSILT
     VLLTLMIGLV LASVVQWEEL KGRAIYRVLL ILPYAVPAFI SILIFKGLFN QSFGEINMVL
     NALFGISPSW FSDPIMAKSM VLIVNTWLGF PYMMILCMGL LKAIPEDLYE ASAIDGANFV
     QNFTRVTLPL MIKPLTPLLI ASFAFNFNNF VMIQLLTQGG PNMIGTSEPA GYTDLLVSYT
     YRIAFEGGGG QDFGLASAIA TLIFLLVGAL ALLNLRFTKL SQN