MALF_SHIFL
ID MALF_SHIFL Reviewed; 514 AA.
AC Q83P81;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000250|UniProtKB:P02916};
GN Name=malF; OrderedLocusNames=SF4172, S3559;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN45593.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18606.1; -; Genomic_DNA.
DR RefSeq; NP_709886.2; NC_004337.2.
DR AlphaFoldDB; Q83P81; -.
DR BMRB; Q83P81; -.
DR SMR; Q83P81; -.
DR STRING; 198214.SF4172; -.
DR EnsemblBacteria; AAN45593; AAN45593; SF4172.
DR EnsemblBacteria; AAP18606; AAP18606; S3559.
DR GeneID; 1023460; -.
DR KEGG; sfl:SF4172; -.
DR KEGG; sfx:S3559; -.
DR PATRIC; fig|198214.7.peg.4922; -.
DR HOGENOM; CLU_016047_20_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; 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_0000060075"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 35..37
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 59..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 92..276
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 298..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 341..371
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 393..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 438..483
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 505..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 410
FT /note="L -> P (in Ref. 2; AAP18606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 57029 MW; 939D5CC2EB789DA7 CRC64;
MDVIKKKHWW QSDALKWSVL GLLGLLVGYL VVLMYAQGEY LFAITTLILS SAGLYIFANR
KAYAWRYVYP GMAGMGLFVL FPLVCTIAIA FTNYSSTNQL TFERAQEVLL DRSWQAGKTY
NFGLYPAGDE WQLALSDGET GKNYLSDAFK FGGEQKLQLK ETTAQPEGER ANLRVITQNR
QALSDITAIL PDGNKVMMSS LRQFSGTQPL YTLDGDGTLT NNQSGVKYRP NNQIGFYQSI
TADGNWGDEK LSPGYTVTTG WKNFTRVFTD EGIQKPFLAI FVWTVVFSLI TVFLTVAVGM
VLACLVQWEA LRGKAVYRVL LILPYAVPSF ISILIFKGLF NQSFGEINMM LSALFGVKPA
WFSDPTTART MLIIVNTWLG YPYMMILCMG LLKAIPDDLY EASAMDGAGL FQNFFKITLP
LLIKPLTPLM IASFAFNFNN FVLIQLLTNG GPDRLGTTTP AGYTDLLVNY TYRIAFEGGG
GQDFGLAAAI ATLIFLLVGA LAIVNLKATR MKFD