MALG_ECO57
ID MALG_ECO57 Reviewed; 296 AA.
AC P68185; P07622;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalG {ECO:0000250|UniProtKB:P68183};
GN Name=malG; OrderedLocusNames=Z5630, ECs5015;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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:P68183}.
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:P68183}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P68183}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P68183}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. MalFG subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG59231.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38438.1; -; Genomic_DNA.
DR PIR; C86096; C86096.
DR PIR; G91255; G91255.
DR RefSeq; NP_313042.1; NC_002695.1.
DR RefSeq; WP_001252058.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P68185; -.
DR SMR; P68185; -.
DR STRING; 155864.EDL933_5369; -.
DR EnsemblBacteria; AAG59231; AAG59231; Z5630.
DR GeneID; 66672053; -.
DR KEGG; ece:Z5630; -.
DR PATRIC; fig|386585.9.peg.5238; -.
DR eggNOG; COG3833; Bacteria.
DR HOGENOM; CLU_016047_1_2_6; -.
DR OMA; NTYLMYG; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 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..296
FT /note="Maltose/maltodextrin transport system permease
FT protein MalG"
FT /id="PRO_0000060083"
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..88
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 112..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..143
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 144..152
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..175
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 176..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 228..257
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 281..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 85..281
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 296 AA; 32225 MW; E54418E91E344A29 CRC64;
MAMVQPKSQK ARLFITHLLL LLFIAAIMFP LLMVVAISLR QGNFATGSLI PEQISWDHWK
LALGFSVEQA DGRITPPPFP VLLWLWNSVK VAGISAIGIV ALSTTCAYAF ARMRFPGKAT
LLKGMLIFQM FPAVLSLVAL YALFDRLGEY IPFIGLNTHG GVIFAYLGGI ALHVWTIKGY
FETIDSSLEE AAALDGATPW QAFRLVLLPL SVPILAVVFI LSFIAAITEV PVASLLLRDV
NSYTLAVGMQ QYLNPQNYLW GDFAAAAVMS ALPITIVFLL AQRWLVNGLT AGGVKG
