ID   MALG_VIBCH              Reviewed;         296 AA.
AC   Q9KL07;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Maltose/maltodextrin transport system permease protein MalG {ECO:0000250|UniProtKB:P68183};
GN   Name=malG; OrderedLocusNames=VC_A0943;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003853; AAF96839.1; -; Genomic_DNA.
DR   PIR; F82397; F82397.
DR   RefSeq; NP_233327.1; NC_002506.1.
DR   RefSeq; WP_001252027.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KL07; -.
DR   SMR; Q9KL07; -.
DR   STRING; 243277.VC_A0943; -.
DR   DNASU; 2612568; -.
DR   EnsemblBacteria; AAF96839; AAF96839; VC_A0943.
DR   GeneID; 57742308; -.
DR   GeneID; 57992373; -.
DR   GeneID; 66941007; -.
DR   KEGG; vch:VC_A0943; -.
DR   PATRIC; fig|243277.26.peg.3555; -.
DR   eggNOG; COG3833; Bacteria.
DR   HOGENOM; CLU_016047_1_2_6; -.
DR   OMA; AWLLKGY; -.
DR   BioCyc; VCHO:VCA0943-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
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_0000060089"
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;  32182 MW;  D0E8E47A98BDC528 CRC64;
     MAMVQGKSLK YRVWATHAAL WVFLALIIFP LLMIVAISFR EGNFATGSLI PDRPSLEHWK
     LALGIAVQNA DGSVTPPPFP VMTWLWNSVK VAGITSVLIV ALSTTSAYAF ARMRFKGKET
     ILKAMMIFQM FPAVLALVAL YALFDKLGQY IPFLGLNTHG GLIFSYLGGI ALHVWTIKGY
     FETIDRSLEE AAALDGATPW QAFRLVLLPL SVPILAVVFI LSFIGVVGEV PVASLLLSDV
     NSYTLAVGMQ QYLYPQNYLW GDFAAAAVLS ALPITIVFLL AQRWLVGGLT AGGVKG