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MALG_SHIFL
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   25-MAY-2022, entry version 102.
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; 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: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   EnsemblBacteria; AAN45594; AAN45594; SF4173.
DR   EnsemblBacteria; AAP18605; AAP18605; S3558.
DR   GeneID; 1025406; -.
DR   GeneID; 66672053; -.
DR   KEGG; sfl:SF4173; -.
DR   KEGG; sfx:S3558; -.
DR   PATRIC; fig|198214.7.peg.4923; -.
DR   HOGENOM; CLU_016047_1_2_6; -.
DR   OMA; NTYLMYG; -.
DR   OrthoDB; 1510342at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_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
 
 
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