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 27-MAR-2024, entry version 112.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN Name=malF;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Pseudomonadota; 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; IITQNRQ; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 2.40.430.10; D-maltodextrin-binding protein, MBP; 1.
DR Gene3D; 1.20.58.370; MalF N-terminal region-like; 1.
DR Gene3D; 3.10.650.10; MalF N-terminal region-like; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR035277; MalF_N.
DR InterPro; IPR048464; MalF_N_TM.
DR InterPro; IPR029345; MalF_P2.
DR InterPro; IPR047103; MalF_P2_sf.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR47314; MALTOSE/MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALF; 1.
DR PANTHER; PTHR47314:SF1; MALTOSE_MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALF; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF20872; MalF_N_TM; 1.
DR Pfam; PF14785; MalF_P2; 1.
DR SUPFAM; SSF160964; MalF N-terminal region-like; 1.
DR SUPFAM; SSF161098; MetI-like; 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
//
