ID   MALF_KLEAE              Reviewed;         514 AA.
AC   P18812;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN   Name=malF;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2674653; DOI=10.1007/bf00331269;
RA   Dahl M.K., Francoz E., Saurin W., Boos W., Manson M.D., Hofnung M.;
RT   "Comparison of sequences from the malB regions of Salmonella typhimurium
RT   and Enterobacter aerogenes with Escherichia coli K12: a potential new
RT   regulatory site in the interoperonic region.";
RL   Mol. Gen. Genet. 218:199-207(1989).
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   PIR; S05332; S05332.
DR   RefSeq; WP_015368773.1; NZ_WPHE01000008.1.
DR   AlphaFoldDB; P18812; -.
DR   SMR; P18812; -.
DR   STRING; 548.EAG7_03821; -.
DR   GeneID; 66606010; -.
DR   OMA; DGHNSTK; -.
DR   OrthoDB; 1619224at2; -.
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; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..514
FT                   /note="Maltose/maltodextrin transport system permease
FT                   protein MalF"
FT                   /id="PRO_0000060071"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        36..39
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        58..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        93..283
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        307..318
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        342..369
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        393..412
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        436..483
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        507..514
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          281..505
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   514 AA;  56895 MW;  FBBBE7154E1D01DF CRC64;
     MDAVKKKHWW QSPQLTWSVI GLLCLLVGYL VVLMYAQGEY LFAIMTLILS SVGLYIFSNR
     KAYAWRYVYP GLAGMGLFVL FPLICTIAIA FTNYSSTNQL TFERAQQVLM DRSFQAGKAY
     NFSLYPAGDE WQLALTDGES GKNYLSEAFK FGGEQKLALK EADALPQGER ANLRVITQNR
     AALNQLTAVL PDESKVIMSS LRQFSGTQPL YALANDGTLT NNQSGVKYRP NADIGFYQSI
     NADGSWGNEK LSPGYTVTIG WDNFTRVFQD EGIQKPFFAI FVWTVVFSVL TVILTVAVGM
     VLACLVQWEA LKGKAIYRVL LILPYAVPSF ISILIFKGLF NQSFGEINMM LSALFGIKPA
     WFSDPTTART MIIIVNTWLG YPYMMILCMG LLKAIPDDLY EASAMDGAGP FQNFFKITLP
     LLIKPLTPLM IASFAFNFNN FVLIQLLTNG GPDRLGTTTP AGYTDLLVSY TYRIAFEGGG
     GQDFGLAAAI ATLIFLLVGA LAIVNLKATR MKFD