ID MALG_SHIFL Reviewed; 296 AA.
AC P68186; P07622;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalG {ECO:0000250|UniProtKB:P68183};
GN Name=malG; OrderedLocusNames=SF4173, S3558;
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; 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: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; AE005674; AAN45594.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18605.1; -; Genomic_DNA.
DR RefSeq; NP_709887.1; NC_004337.2.
DR RefSeq; WP_001252058.1; NZ_WPGW01000079.1.
DR AlphaFoldDB; P68186; -.
DR SMR; P68186; -.
DR STRING; 198214.SF4173; -.
DR PaxDb; 198214-SF4173; -.
DR GeneID; 1025406; -.
DR GeneID; 83579060; -.
DR KEGG; sfl:SF4173; -.
DR KEGG; sfx:S3558; -.
DR PATRIC; fig|198214.7.peg.4923; -.
DR HOGENOM; CLU_016047_1_2_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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; MetI-like; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR32243; MALTOSE TRANSPORT SYSTEM PERMEASE-RELATED; 1.
DR PANTHER; PTHR32243:SF50; MALTOSE_MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALG; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; MetI-like; 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_0000060088"
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
//
