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MGLA_CLOPE
ID   MGLA_CLOPE              Reviewed;         515 AA.
AC   Q8XKQ2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=CPE1342;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MglA),
CC       two 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; BA000016; BAB81048.1; -; Genomic_DNA.
DR   RefSeq; WP_011010399.1; NC_003366.1.
DR   AlphaFoldDB; Q8XKQ2; -.
DR   STRING; 195102.gene:10490605; -.
DR   EnsemblBacteria; BAB81048; BAB81048; BAB81048.
DR   KEGG; cpe:CPE1342; -.
DR   HOGENOM; CLU_000604_92_3_9; -.
DR   OMA; RIDHKAT; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043211; F:ABC-type carbohydrate transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015862; ABC_transpr_MglA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43790:SF7; PTHR43790:SF7; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 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..515
FT                   /note="Galactose/methyl galactoside import ATP-binding
FT                   protein MglA"
FT                   /id="PRO_0000261359"
FT   DOMAIN          8..243
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   DOMAIN          254..499
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   515 AA;  57668 MW;  810ACA7A728037F1 CRC64;
     MKDSSNLLEM RNISKEFPGV KALDNVTLKV KKGSVHALMG ENGAGKSTLM KCLFGIYHPN
     SGEIFISGQK VQFKNSKHAL DNGVSMVHQE LNQVRERNVM DNLWLGRYPK KGLFIDEKKM
     YDETEKIFKD LDINVNPRDK VSTLSVSQMQ MVEIAKAVSY NSKIIVMDEP TSSLTEKEVS
     HLFKIINKLR KQGISIIYIS HKMEEILEIS DEVTIMRDGK WIATEKASDL TMDLIIKLMV
     GRELTDRFPK KDHIPKETTL EVNNLSDAKN ELKNVSFKLR KGEILGIAGL VGAKRTETLE
     TLFGLREKGS GDIILHGKKV DNSKPFKAMQ NGFALVTEER RQTGIFGKLP IDFNSIIANI
     DSYKTSTGLL ANERISKDTQ WVIDSMKVKT PSQKTLIGSL SGGNQQKIVI GKWLLRKPEI
     LLLDEPTRGI DVGAKFEIYQ LINELAKEDK GIIMVSSEMP ELLGVCDRIL VMSNGRVSGI
     VNANETTQEE IMHLSAKYLS VTGGVNNANQ IKEKV
 
 
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