MALF_SALTY
ID MALF_SALTY Reviewed; 514 AA.
AC P26467;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN Name=malF; OrderedLocusNames=STM4228;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1730061; DOI=10.1016/0167-4781(92)90492-i;
RA Schneider E., Francoz E., Dassa E.;
RT "Completion of the nucleotide sequence of the 'maltose B' region in
RT Salmonella typhimurium: the high conservation of the malM gene suggests a
RT selected physiological role for its product.";
RL Biochim. Biophys. Acta 1129:223-227(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; X54292; CAA38190.1; -; Genomic_DNA.
DR EMBL; M33921; AAA27159.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23052.1; -; Genomic_DNA.
DR PIR; S20604; S20604.
DR RefSeq; NP_463093.1; NC_003197.2.
DR RefSeq; WP_000382573.1; NC_003197.2.
DR AlphaFoldDB; P26467; -.
DR SMR; P26467; -.
DR STRING; 99287.STM4228; -.
DR PaxDb; P26467; -.
DR EnsemblBacteria; AAL23052; AAL23052; STM4228.
DR GeneID; 1255754; -.
DR KEGG; stm:STM4228; -.
DR PATRIC; fig|99287.12.peg.4448; -.
DR HOGENOM; CLU_016047_20_0_6; -.
DR OMA; DGHNSTK; -.
DR PhylomeDB; P26467; -.
DR BioCyc; SENT99287:STM4228-MON; -.
DR Proteomes; UP000001014; 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 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..514
FT /note="Maltose/maltodextrin transport system permease
FT protein MalF"
FT /id="PRO_0000060074"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 37..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"
FT CONFLICT 242
FT /note="A -> G (in Ref. 1; CAA38190)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="I -> S (in Ref. 1; CAA38190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 56967 MW; 79724A512A21C30C CRC64;
MDVIKKKHWW QSDQLKWSVI GLLGLLVGYL VVLMYVQGEY LFAIMTLILS SAGLYIFANR
KTYAWRYVYP GLAGMGLFVL FPLVCTIAIA FTNYSSTNQL TFERAQQVLM DRSYQAGKTY
NFGLYPTGDE WQLALTDGET GKHYLSDAFS FGGEQKLQLK ETDALPGGER ANLRIITQNR
LALNQITAVL PDESKVIMSS LRQFSGTRPL YTLADDGLLT NNQSGVKYRP NNDSGYYQSI
NADGSWGDEK LSPGYTVTIG AKNFTRVFTD EGIQKPFFAI FVWTVVFSVL TVVLTVAVGM
VLACLVQWEA LKGKAIYRVL LILPYAVPSF ISILIFKGLF NQSFGEINMM LSALFGIKPA
WFSDPNTARA MVIIVNTWLG YPYMMILCMG LLKAIPDDLY EASAMDGAGP FQNFFKITLP
LLIKPLTPLM IASFAFNFNN FVLIQLLTNG GPDRLGTTTP AGYTDLLVSY TYRIAFEGGG
GQDFGLAAAI ATLIFLLVGA LAIVNLKATR MKFD
