MALF_ECOL6
ID MALF_ECOL6 Reviewed; 519 AA.
AC Q8FB38;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN Name=malF; OrderedLocusNames=c5003;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83429.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FB38; -.
DR BMRB; Q8FB38; -.
DR SMR; Q8FB38; -.
DR STRING; 199310.c5003; -.
DR EnsemblBacteria; AAN83429; AAN83429; c5003.
DR KEGG; ecc:c5003; -.
DR eggNOG; COG1175; Bacteria.
DR HOGENOM; CLU_016047_20_0_6; -.
DR OMA; DGHNSTK; -.
DR BioCyc; ECOL199310:C5003-MON; -.
DR Proteomes; UP000001410; Chromosome.
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..519
FT /note="Maltose/maltodextrin transport system permease
FT protein MalF"
FT /id="PRO_0000060070"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..41
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 42..44
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..62
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 63..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 98..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..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 347..374
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 398..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..440
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 441..488
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..511
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 512..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 286..510
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 519 AA; 57638 MW; F881A974B6CC175C CRC64;
MRKNPMDVIK KKHWWQSDAL KWSVLGLLGL LVGYLVVLMY AQGEYLFAIT TLILSSAGLY
IFANRKAYAW RYVYPGMAGM GLFVLFPLVC TIAIAFTNYS STNQLTFERA QEVLLDRSWQ
AGKIYNFGLY PAGDEWQLAL SDGETGKNYL SDAFKFGGEQ KLQLKESATQ PEGERANLRV
ITQNRQALSD ITAILPDGNK VMMSSLRQFS GTQPLYTLDG DGTLTNNQSG VKYRPNNQIG
FYQSITADGN WGDEKLSPGY TVTTGWKNFT RVFTDEGIQK PFLAIFVWTV VFSLITVFLT
VAVGMVLACL VQWEALRGKA VYRVLLILPY AVPSFISILI FKGLFNQSFG EINMMLSALF
GVKPAWFSDP TTARTMLIIV NTWLGYPYMM ILCMGLLKAI PDDLYEASAM DGAGPFQNFF
KITLPLLIKP LTPLMIASFA FNFNNFVLIQ LLTNGGPDRL GTTTPAGYTD LLVNYTYRIA
FEGGGGQDFG LAAAIATLIF LLVGALAIVN LKATRMKFD
