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MGLA_ECOLI
ID   MGLA_ECOLI              Reviewed;         506 AA.
AC   P0AAG8; P23199; P76442; Q2MAT0;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 129.
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};
GN   OrderedLocusNames=b2149, JW2136;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1719366; DOI=10.1007/bf00267469;
RA   Hogg R.W., Voelker C., von Carlowitz I.;
RT   "Nucleotide sequence and analysis of the mgl operon of Escherichia coli
RT   K12.";
RL   Mol. Gen. Genet. 229:453-459(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RC   STRAIN=K12;
RX   PubMed=3302609; DOI=10.1007/bf00330450;
RA   Scholle A., Vreemann J., Blank V., Nold A., Boos W., Manson M.D.;
RT   "Sequence of the mglB gene from Escherichia coli K12: comparison of wild-
RT   type and mutant galactose chemoreceptors.";
RL   Mol. Gen. Genet. 208:247-253(1987).
RN   [5]
RP   FUNCTION IN GALACTOSE AND METHYL GALACTOSIDE TRANSPORT.
RX   PubMed=4910389; DOI=10.1111/j.1432-1033.1970.tb00956.x;
RA   Boos W., Sarvas M.O.;
RT   "Close linkage between a galactose binding protein and the beta-
RT   methylgalactoside permease in Escherichia coli.";
RL   Eur. J. Biochem. 13:526-533(1970).
RN   [6]
RP   FUNCTION IN METHYL GALACTOSIDE TRANSPORT.
RX   PubMed=6807987; DOI=10.1016/s0021-9258(18)34236-4;
RA   Rotman B., Guzman R.;
RT   "Identification of the mglA gene product in the beta-methylgalactoside
RT   transport system of Escherichia coli using plasmid DNA deletions generated
RT   in vitro.";
RL   J. Biol. Chem. 257:9030-9034(1982).
RN   [7]
RP   SUBCELLULAR LOCATION, AND FUNCTION IN GALACTOSE TRANSPORT.
RC   STRAIN=K12;
RX   PubMed=6294056; DOI=10.1128/jb.153.1.408-415.1983;
RA   Harayama S., Bollinger J., Iino T., Hazelbauer G.L.;
RT   "Characterization of the mgl operon of Escherichia coli by transposon
RT   mutagenesis and molecular cloning.";
RL   J. Bacteriol. 153:408-415(1983).
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 (Probable). {ECO:0000305|PubMed:4910389,
CC       ECO:0000305|PubMed:6294056, ECO:0000305|PubMed:6807987}.
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 inner membrane {ECO:0000305|PubMed:6294056};
CC       Peripheral membrane protein {ECO:0000305|PubMed:6294056}.
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; M59444; AAA24170.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75210.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76626.1; -; Genomic_DNA.
DR   EMBL; X05646; CAA29133.1; -; Genomic_DNA.
DR   PIR; D64983; D64983.
DR   RefSeq; NP_416654.1; NC_000913.3.
DR   RefSeq; WP_000255039.1; NZ_SSZK01000011.1.
DR   AlphaFoldDB; P0AAG8; -.
DR   SMR; P0AAG8; -.
DR   BioGRID; 4260868; 26.
DR   BioGRID; 853280; 6.
DR   ComplexPortal; CPX-4341; Beta-methyl-D-galactoside/galactose ABC transporter complex.
DR   IntAct; P0AAG8; 13.
DR   STRING; 511145.b2149; -.
DR   TCDB; 3.A.1.2.3; the atp-binding cassette (abc) superfamily.
DR   jPOST; P0AAG8; -.
DR   PaxDb; P0AAG8; -.
DR   PRIDE; P0AAG8; -.
DR   EnsemblBacteria; AAC75210; AAC75210; b2149.
DR   EnsemblBacteria; BAE76626; BAE76626; BAE76626.
DR   GeneID; 66673955; -.
DR   GeneID; 949036; -.
DR   KEGG; ecj:JW2136; -.
DR   KEGG; eco:b2149; -.
DR   PATRIC; fig|1411691.4.peg.92; -.
DR   EchoBASE; EB0587; -.
DR   eggNOG; COG1129; Bacteria.
DR   HOGENOM; CLU_000604_92_3_6; -.
DR   InParanoid; P0AAG8; -.
DR   OMA; IKMLSGA; -.
DR   PhylomeDB; P0AAG8; -.
DR   BioCyc; EcoCyc:MGLA-MON; -.
DR   BioCyc; MetaCyc:MGLA-MON; -.
DR   PRO; PR:P0AAG8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0043211; F:ABC-type carbohydrate transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR   GO; GO:0005354; F:galactose transmembrane transporter activity; IMP:EcoCyc.
DR   GO; GO:0015592; F:methylgalactoside transmembrane transporter activity; IMP:EcoCyc.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0015757; P:galactose transmembrane transport; IMP:EcoCyc.
DR   GO; GO:0015765; P:methylgalactoside transport; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Sugar transport;
KW   Translocase; Transport.
FT   CHAIN           1..506
FT                   /note="Galactose/methyl galactoside import ATP-binding
FT                   protein MglA"
FT                   /id="PRO_0000092512"
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"
FT   CONFLICT        57..69
FT                   /note="KCLFGIYQKDSGT -> NACLVFIKRLRH (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="A -> G (in Ref. 2; AAA24170)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   506 AA;  56415 MW;  15F794D57E386BCF CRC64;
     MVSSTTPSSG EYLLEMSGIN KSFPGVKALD NVNLKVRPHS IHALMGENGA GKSTLLKCLF
     GIYQKDSGTI LFQGKEIDFH SAKEALENGI SMVHQELNLV LQRSVMDNMW LGRYPTKGMF
     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 KNKVGLLDNS RMKSDTQWVI DSMRVKTPGH RTQIGSLSGG NQQKVIIGRW
     LLTQPEILML DEPTRGIDVG AKFEIYQLIA ELAKKGKGII IISSEMPELL GITDRILVMS
     NGLVSGIVDT KTTTQNEILR LASLHL
 
 
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