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Database: UniProt
Entry: Q31YV7
LinkDB: Q31YV7
Original site: Q31YV7 
ID   MGLA_SHIBS              Reviewed;         506 AA.
AC   Q31YV7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Galactose/methyl galactoside import ATP-binding protein MglA {ECO:0000255|HAMAP-Rule:MF_01717};
DE            EC=7.5.2.11 {ECO:0000255|HAMAP-Rule:MF_01717};
GN   Name=mglA {ECO:0000255|HAMAP-Rule:MF_01717}; OrderedLocusNames=SBO_2178;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Part of the ABC transporter complex MglABC involved in
CC       galactose/methyl galactoside import. Responsible for energy coupling to
CC       the transport system. {ECO:0000255|HAMAP-Rule:MF_01717}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:60156, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.5.2.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01717};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60157;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01717};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + methyl beta-D-galactoside(out) = ADP + H(+) +
CC         methyl beta-D-galactoside(in) + phosphate; Xref=Rhea:RHEA:72531,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17540,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01717};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72532;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01717};
CC   -!- SUBUNIT: The complex is composed of one ATP-binding protein (MglA), two
CC       transmembrane proteins (MglC) and a solute-binding protein (MglB).
CC       {ECO:0000255|HAMAP-Rule:MF_01717}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01717}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01717}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Galactose/methyl galactoside importer (TC 3.A.1.2.3) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01717}.
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DR   EMBL; CP000036; ABB66751.1; -; Genomic_DNA.
DR   RefSeq; WP_000255052.1; NC_007613.1.
DR   AlphaFoldDB; Q31YV7; -.
DR   SMR; Q31YV7; -.
DR   KEGG; sbo:SBO_2178; -.
DR   HOGENOM; CLU_000604_92_3_6; -.
DR   Proteomes; UP000007067; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   CDD; cd03216; ABC_Carb_Monos_I; 1.
DR   CDD; cd03215; ABC_Carb_Monos_II; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43790; CARBOHYDRATE TRANSPORT ATP-BINDING PROTEIN MG119-RELATED; 1.
DR   PANTHER; PTHR43790:SF7; GALACTOSE_METHYL GALACTOSIDE IMPORT ATP-BINDING PROTEIN MGLA; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS51260; MGLA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..506
FT                   /note="Galactose/methyl galactoside import ATP-binding
FT                   protein MglA"
FT                   /id="PRO_0000261373"
FT   DOMAIN          14..249
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   DOMAIN          264..506
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ   SEQUENCE   506 AA;  56528 MW;  366778425B4FAF9D CRC64;
     MVSSTTPSSG EYLLEMSGIN KSFPGVKALD NVNLKVRPHS IHALMGENGA GKSTLLKCLF
     GIYQKDSGTI LFQGKEIDFH SAKEALENGI SMVHQELNLV LQRSVMDNMW LRRYPTKGMF
     VDQDKMYRET KAIFDELDID IDPRARVGTL SVSQMQMIEI AKAFSYNAKI VIMDEPTSSL
     TEKEVNHLFT IIRKLKERGC GIVYISHKME EIFQLCDEVT VLRDGQWIAT EPLAGLTMDK
     IIAMMVGRSL NQRFPDKENK PGEVILEVRN LTSLRQPSIR DVSFDLHKGE ILGIAGLVGA
     KRTDIVETLF GIREKSAGTI TLHGKQINNH NANEAINHGF ALVTEERRST GIYAYLDIGF
     NSLISNIRNY KNKVGLLDKS RMKSDTQWVI DSMRVKTPGH RTQIGSLSGG NQQKVIIGRW
     LLTQPEILML DEPTRGIDVG AKFEIYQLIA ELAKKGKGII IISSEMPELL GITDRILVMS
     NGLVSGIVDT KTTTQNEILR LASLHL
//
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