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Database: UniProt
Entry: Q896Y2
LinkDB: Q896Y2
Original site: Q896Y2 
ID   MGLA_CLOTE              Reviewed;         504 AA.
AC   Q896Y2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 137.
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=CTC_00861;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01717};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; AE015927; AAO35458.1; -; Genomic_DNA.
DR   RefSeq; WP_011099120.1; NC_004557.1.
DR   AlphaFoldDB; Q896Y2; -.
DR   SMR; Q896Y2; -.
DR   STRING; 212717.CTC_00861; -.
DR   GeneID; 24253069; -.
DR   KEGG; ctc:CTC_00861; -.
DR   HOGENOM; CLU_000604_92_3_9; -.
DR   OrthoDB; 9771863at2; -.
DR   Proteomes; UP000001412; 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 membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..504
FT                   /note="Galactose/methyl galactoside import ATP-binding
FT                   protein MglA"
FT                   /id="PRO_0000261362"
FT   DOMAIN          8..247
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   DOMAIN          258..504
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ   SEQUENCE   504 AA;  56052 MW;  EC28FF9596DD5D2D CRC64;
     MVENNIILEM NGISKNFPGV KALDGVDLKV KKGTVHALMG ENGAGKSTLM KCLFGIYRSD
     DGEIVLGGKK VQFKNAKDAL ENGISMIHQE LHPVPHRSVM ENVWLGRFPV KKVFGLGIVD
     HKKMYEDTKD LLGKLKMNID PNTLVSKLSV SQVQGLEIAK AVSYNSKIIV MDEPTSSLTE
     NEVTHLFNII SDLKNQGVAI IYISHKMEEI LKIADEVTIM RDGKYIGTWE AEGLTTDLII
     SKMVGRDLTN RFPPKENTPG EVIMKVENLT SANNKSFKDI SFELRKGEIL GIGGLVGAQR
     TELVESIFGL RKIETGKIYI NGQEVKIKSP INSKKYGIAL LTEERRSTGI FPVLTVGDNT
     IIAGLDKYID LKFVVNQKRG MKDIKNSIEK LNIRTPSHAT QIKNLSGGNQ QKVIFSRWLL
     TEPDVLIMDE PTRGIDVGAK YEIYSIISDL SKMGKSIIMI SSEMPELIGM SDRIMIMCDG
     RLSGIIEGEE ATQEEIMKYA TRFI
//
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