MALG_SALTY
ID MALG_SALTY Reviewed; 296 AA.
AC P26468;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalG {ECO:0000250|UniProtKB:P68183};
GN Name=malG; OrderedLocusNames=STM4227;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1730061; DOI=10.1016/0167-4781(92)90492-i;
RA Schneider E., Francoz E., Dassa E.;
RT "Completion of the nucleotide sequence of the 'maltose B' region in
RT Salmonella typhimurium: the high conservation of the malM gene suggests a
RT selected physiological role for its product.";
RL Biochim. Biophys. Acta 1129:223-227(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2284499; DOI=10.1016/0923-2508(90)90058-x;
RA Francoz E., Schneider E., Dassa E.;
RT "The sequence of the malG gene from Salmonella typhimurium and its
RT functional implications.";
RL Res. Microbiol. 141:633-644(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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}.
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DR EMBL; X54292; CAA38191.1; -; Genomic_DNA.
DR EMBL; M33921; AAA27160.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23051.1; -; Genomic_DNA.
DR PIR; A60175; A60175.
DR RefSeq; NP_463092.1; NC_003197.2.
DR RefSeq; WP_001252085.1; NC_003197.2.
DR AlphaFoldDB; P26468; -.
DR SMR; P26468; -.
DR STRING; 99287.STM4227; -.
DR PaxDb; P26468; -.
DR EnsemblBacteria; AAL23051; AAL23051; STM4227.
DR GeneID; 1255753; -.
DR KEGG; stm:STM4227; -.
DR PATRIC; fig|99287.12.peg.4447; -.
DR HOGENOM; CLU_016047_1_2_6; -.
DR OMA; AWLLKGY; -.
DR PhylomeDB; P26468; -.
DR BioCyc; SENT99287:STM4227-MON; -.
DR Proteomes; UP000001014; 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:0015423; F:ABC-type maltose transporter activity; IBA:GO_Central.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IBA:GO_Central.
DR GO; GO:0015768; P:maltose transport; IBA:GO_Central.
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_0000060087"
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; 4CFE814CD60258CC CRC64;
MAMVQPKSQK LRLLITHLGL LIFIAAIMFP LLMVIAISLR EGNFATGSLI PDKISWEHWR
LALGFSVEHA DGRVTPPPFP VLLWLWNSVK IAGITAIGIV ALSTTCAYAF ARMRFPGKAT
LLKGMLIFQM FPAVLSLVAL YALFDRLGQY IPFIGLNTHG GVIFAYLGGI ALHVWTIKGY
FETIDSSLEE AAALDGATPW QAFRLVLLPL SVPILAVVFI LSFIAAITEV PVASLLLRDV
DSYTLAVGMQ QYLNPQNYLW GDFAAAAVLS AIPITLVFLL AQRWLVNGLT AGGVKG
