MALF_VIBPA
ID MALF_VIBPA Reviewed; 524 AA.
AC Q87GB7;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN Name=malF; OrderedLocusNames=VPA1400;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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; BA000032; BAC62743.1; -; Genomic_DNA.
DR RefSeq; NP_800910.1; NC_004605.1.
DR RefSeq; WP_011106507.1; NC_004605.1.
DR AlphaFoldDB; Q87GB7; -.
DR SMR; Q87GB7; -.
DR STRING; 223926.28809768; -.
DR EnsemblBacteria; BAC62743; BAC62743; BAC62743.
DR GeneID; 1192096; -.
DR KEGG; vpa:VPA1400; -.
DR PATRIC; fig|223926.6.peg.4325; -.
DR eggNOG; COG1175; Bacteria.
DR HOGENOM; CLU_016047_20_0_6; -.
DR OMA; DGHNSTK; -.
DR Proteomes; UP000002493; Chromosome 2.
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..524
FT /note="Maltose/maltodextrin transport system permease
FT protein MalF"
FT /id="PRO_0000060077"
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..290
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 314..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 346..379
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 403..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..458
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 459..493
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..516
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 517..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 291..515
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 524 AA; 57644 MW; BB59B0D3410FA7F6 CRC64;
MQSVQGTNAM TAPEASLPSS KKVFIKWSLL GTVGILNGYA TILMYSRGEI AFALLTIILT
ALALFIFGSK KTYAHRYIYP GIAGMILFIL FPLAYTIGLA FTNYSAKNQL SFDRAQSVLL
DRTYQSGDSY PFTLYNTDQG HQIVVEKDGE LLATPVFQLQ GFSETDLDLA PITEAAGDKE
PIKTIVKNRT ALSSVDLHLP NGDDIRMSGL RKFAAVVPLY TLQEDGETLY NNRTQETLRP
NMEVGYYQPV DENGQFVGST VSPGFVVNIG THNFERVWKD DGIKEPFISI FIWTIVFSAL
TVVCTLVIGL VLASVVQWEA LKGRSIYRLL LILPYAVPAF ISILIFKGLF NQSFGEINML
LEGLFGISPA WFSDPFMAKT MILIVNTWLG FPYMMILCMG LLKAIPDDLY EASAIDGANF
ITNFTRITMP MMLKPLTPLL IASFAFNFNN FVLIQLLTGG GPNMIGTSEP AGYTDLLVSY
TYRIAFEGAG GQDFGLASAV ATLIFLLVGA LALINLRVTK VAQD
