MALG_ECOLI
ID MALG_ECOLI Reviewed; 296 AA.
AC P68183; P07622; Q2M6S2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalG {ECO:0000305};
GN Name=malG {ECO:0000303|PubMed:3000770}; OrderedLocusNames=b4032, JW3992;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3000770; DOI=10.1002/j.1460-2075.1985.tb03928.x;
RA Dassa E., Hofnung M.;
RT "Sequence of gene malG in E. coli K12: homologies between integral membrane
RT components from binding protein-dependent transport systems.";
RL EMBO J. 4:2287-2293(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-296.
RC STRAIN=K12;
RX PubMed=2820984; DOI=10.1016/s0021-9258(18)47883-0;
RA Davis E.O., Henderson P.J.F.;
RT "The cloning and DNA sequence of the gene xylE for xylose-proton symport in
RT Escherichia coli K12.";
RL J. Biol. Chem. 262:13928-13932(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-296.
RC STRAIN=K12;
RX PubMed=2836810; DOI=10.1093/nar/16.9.4097;
RA Francoz E., Dassa E.;
RT "3' end of the malEFG operon in E.coli: localization of the transcription
RT termination site.";
RL Nucleic Acids Res. 16:4097-4109(1988).
RN [7]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=2155217; DOI=10.1016/s0021-9258(19)39555-9;
RA Davidson A.L., Nikaido H.;
RT "Overproduction, solubilization, and reconstitution of the maltose
RT transport system from Escherichia coli.";
RL J. Biol. Chem. 265:4254-4260(1990).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=2233678; DOI=10.1007/bf00283019;
RA Dassa E.;
RT "Cellular localization of the MalG protein from the maltose transport
RT system in Escherichia coli K12.";
RL Mol. Gen. Genet. 222:33-36(1990).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=2026607; DOI=10.1016/s0021-9258(18)31535-7;
RA Davidson A.L., Nikaido H.;
RT "Purification and characterization of the membrane-associated components of
RT the maltose transport system from Escherichia coli.";
RL J. Biol. Chem. 266:8946-8951(1991).
RN [10]
RP TOPOLOGY.
RX PubMed=8437518; DOI=10.1111/j.1365-2958.1993.tb01094.x;
RA Dassa E., Muir S.;
RT "Membrane topology of MalG, an inner membrane protein from the maltose
RT transport system of Escherichia coli.";
RL Mol. Microbiol. 7:29-38(1993).
RN [11]
RP MUTAGENESIS, AND CHARACTERIZATION.
RX PubMed=8437519; DOI=10.1111/j.1365-2958.1993.tb01095.x;
RA Dassa E.;
RT "Sequence-function relationships in MalG, an inner membrane protein from
RT the maltose transport system in Escherichia coli.";
RL Mol. Microbiol. 7:39-47(1993).
RN [12]
RP MUTAGENESIS OF GLU-190; ALA-192; GLY-196 AND PRO-209.
RX PubMed=9214624; DOI=10.1093/emboj/16.11.3066;
RA Mourez M., Hofnung M., Dassa E.;
RT "Subunit interactions in ABC transporters: a conserved sequence in
RT hydrophobic membrane proteins of periplasmic permeases defines an important
RT site of interaction with the ATPase subunits.";
RL EMBO J. 16:3066-3077(1997).
RN [13]
RP SUBUNIT INTERACTION, AND MUTAGENESIS OF GLU-190; ALA-192 AND GLY-196.
RX PubMed=10809785; DOI=10.1074/jbc.275.20.15526;
RA Hunke S., Mourez M., Jehanno M., Dassa E., Schneider E.;
RT "ATP modulates subunit-subunit interactions in an ATP-binding cassette
RT transporter (MalFGK2) determined by site-directed chemical cross-linking.";
RL J. Biol. Chem. 275:15526-15534(2000).
RN [14]
RP SUBUNIT, SUBCELLULAR LOCATION, AND REQUIREMENT FOR YIDC FOR PROTEIN AND
RP COMPLEX FORMATION.
RX PubMed=18456666; DOI=10.1074/jbc.m801481200;
RA Wagner S., Pop O.I., Haan G.J., Baars L., Koningstein G., Klepsch M.M.,
RA Genevaux P., Luirink J., de Gier J.W.;
RT "Biogenesis of MalF and the MalFGK(2) maltose transport complex in
RT Escherichia coli requires YidC.";
RL J. Biol. Chem. 283:17881-17890(2008).
RN [15]
RP REVIEW.
RX PubMed=9529892; DOI=10.1128/mmbr.62.1.204-229.1998;
RA Boos W., Shuman H.;
RT "Maltose/maltodextrin system of Escherichia coli: transport, metabolism,
RT and regulation.";
RL Microbiol. Mol. Biol. Rev. 62:204-229(1998).
RN [16]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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:0000269|PubMed:2026607,
CC ECO:0000269|PubMed:2155217}.
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). Protein stability and stable complex formation require YidC.
CC {ECO:0000269|PubMed:10809785, ECO:0000269|PubMed:18456666,
CC ECO:0000269|PubMed:2026607, ECO:0000269|PubMed:2155217}.
CC -!- INTERACTION:
CC P68183; P02916: malF; NbExp=5; IntAct=EBI-6400985, EBI-1118919;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:18456666,
CC ECO:0000269|PubMed:2233678}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:18456666,
CC ECO:0000269|PubMed:2233678}.
CC -!- MISCELLANEOUS: When MalF EAA loop mutations are made concomitantly with
CC MalG EAA loop mutations, a complete loss of transport and complex
CC formation is observed. This suggests that the MalF-MalG interaction may
CC be important for the proper assembly and also for the correct function
CC of the transporter.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. MalFG subfamily. {ECO:0000305}.
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DR EMBL; X02871; CAA26628.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43126.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77002.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78034.1; -; Genomic_DNA.
DR EMBL; J02812; AAA79015.1; -; Genomic_DNA.
DR EMBL; X06663; CAA29861.1; -; Genomic_DNA.
DR PIR; A24361; MMECMG.
DR RefSeq; NP_418456.1; NC_000913.3.
DR RefSeq; WP_001252058.1; NZ_STEB01000022.1.
DR PDB; 2R6G; X-ray; 2.80 A; G=1-296.
DR PDB; 3FH6; X-ray; 4.50 A; G/I=1-296.
DR PDB; 3PUV; X-ray; 2.40 A; G=1-296.
DR PDB; 3PUW; X-ray; 2.30 A; G=1-296.
DR PDB; 3PUX; X-ray; 2.30 A; G=1-296.
DR PDB; 3PUY; X-ray; 3.10 A; G=1-296.
DR PDB; 3PUZ; X-ray; 2.90 A; G=1-296.
DR PDB; 3PV0; X-ray; 3.10 A; G=1-296.
DR PDB; 3RLF; X-ray; 2.20 A; G=1-296.
DR PDB; 4JBW; X-ray; 3.91 A; G/I=1-296.
DR PDB; 4KI0; X-ray; 2.38 A; G=1-296.
DR PDBsum; 2R6G; -.
DR PDBsum; 3FH6; -.
DR PDBsum; 3PUV; -.
DR PDBsum; 3PUW; -.
DR PDBsum; 3PUX; -.
DR PDBsum; 3PUY; -.
DR PDBsum; 3PUZ; -.
DR PDBsum; 3PV0; -.
DR PDBsum; 3RLF; -.
DR PDBsum; 4JBW; -.
DR PDBsum; 4KI0; -.
DR AlphaFoldDB; P68183; -.
DR SMR; P68183; -.
DR BioGRID; 4262661; 10.
DR ComplexPortal; CPX-1932; Maltose ABC transporter complex.
DR ComplexPortal; CPX-1978; Enzyme IIA-maltose transport inhibitory complex.
DR DIP; DIP-59709N; -.
DR IntAct; P68183; 5.
DR STRING; 511145.b4032; -.
DR TCDB; 3.A.1.1.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P68183; -.
DR PRIDE; P68183; -.
DR EnsemblBacteria; AAC77002; AAC77002; b4032.
DR EnsemblBacteria; BAE78034; BAE78034; BAE78034.
DR GeneID; 66672053; -.
DR GeneID; 948530; -.
DR KEGG; ecj:JW3992; -.
DR KEGG; eco:b4032; -.
DR PATRIC; fig|1411691.4.peg.2679; -.
DR EchoBASE; EB0551; -.
DR eggNOG; COG3833; Bacteria.
DR HOGENOM; CLU_016047_1_2_6; -.
DR InParanoid; P68183; -.
DR OMA; NTYLMYG; -.
DR PhylomeDB; P68183; -.
DR BioCyc; EcoCyc:MALG-MON; -.
DR BioCyc; MetaCyc:MALG-MON; -.
DR BRENDA; 7.5.2.1; 2026.
DR EvolutionaryTrace; P68183; -.
DR PRO; PR:P68183; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR GO; GO:1990154; C:enzyme IIA-maltose transporter complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:1990060; C:maltose transport complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IDA:EcoCyc.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0015768; P:maltose transport; IDA:EcoCyc.
DR GO; GO:1902344; P:negative regulation of maltose transport; IC:ComplexPortal.
DR GO; GO:0034763; P:negative regulation of transmembrane transport; IC:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..296
FT /note="Maltose/maltodextrin transport system permease
FT protein MalG"
FT /id="PRO_0000060081"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 40..81
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 103..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 145..150
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 172..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 226..259
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 281..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 85..281
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT MUTAGEN 190
FT /note="E->A,C,K,L: Reduction of transport rate."
FT /evidence="ECO:0000269|PubMed:10809785,
FT ECO:0000269|PubMed:9214624"
FT MUTAGEN 192
FT /note="A->D,S,L: Loss of transport and MalK dissociation
FT from the membrane."
FT /evidence="ECO:0000269|PubMed:10809785,
FT ECO:0000269|PubMed:9214624"
FT MUTAGEN 196
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:10809785,
FT ECO:0000269|PubMed:9214624"
FT MUTAGEN 196
FT /note="G->P: Loss of transport and MalK dissociation from
FT the membrane."
FT /evidence="ECO:0000269|PubMed:10809785,
FT ECO:0000269|PubMed:9214624"
FT MUTAGEN 209
FT /note="P->A: No effect."
FT /evidence="ECO:0000269|PubMed:9214624"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:3PUZ"
FT HELIX 12..38
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3PV0"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3PUZ"
FT HELIX 81..112
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2R6G"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4KI0"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:2R6G"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 207..227
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 260..280
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 289..293
FT /evidence="ECO:0007829|PDB:3RLF"
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
