GLTL_ECOLI
ID GLTL_ECOLI Reviewed; 241 AA.
AC P0AAG3; P41076;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glutamate/aspartate import ATP-binding protein GltL {ECO:0000305};
DE EC=7.4.2.1 {ECO:0000305|PubMed:9593292};
GN Name=gltL; OrderedLocusNames=b0652, JW0647;
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 / BK9MDG;
RA Lum D., Wallace B.J.;
RT "Sequence and characterisation of three genes of a glutamate-aspartate
RT binding protein-dependent transport system of Escherichia coli K12.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP REVIEW.
RX PubMed=9593292; DOI=10.1046/j.1365-2958.1998.00764.x;
RA Linton K.J., Higgins C.F.;
RT "The Escherichia coli ATP-binding cassette (ABC) proteins.";
RL Mol. Microbiol. 28:5-13(1998).
CC -!- FUNCTION: Part of the ABC transporter complex GltIJKL involved in
CC glutamate and aspartate uptake. Probably responsible for energy
CC coupling to the transport system. {ECO:0000305|PubMed:9593292}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a polar amino acid(out) + ATP + H2O = a polar amino acid(in) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:14673, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62031, ChEBI:CHEBI:456216; EC=7.4.2.1;
CC Evidence={ECO:0000305|PubMed:9593292};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14674;
CC Evidence={ECO:0000305|PubMed:9593292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamate(out) = ADP + H(+) + L-glutamate(in) +
CC phosphate; Xref=Rhea:RHEA:29035, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:9593292};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29036;
CC Evidence={ECO:0000305|PubMed:9593292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-aspartate(out) = ADP + H(+) + L-aspartate(in) +
CC phosphate; Xref=Rhea:RHEA:29039, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:9593292};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29040;
CC Evidence={ECO:0000305|PubMed:9593292};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GltL),
CC two transmembrane proteins (GltJ and GltK) and a solute-binding protein
CC (GltI). {ECO:0000305|PubMed:9593292}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:9593292};
CC Peripheral membrane protein {ECO:0000305|PubMed:9593292}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U10981; AAA60982.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40853.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73753.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35304.1; -; Genomic_DNA.
DR PIR; B64800; B64800.
DR RefSeq; NP_415185.1; NC_000913.3.
DR RefSeq; WP_000631384.1; NZ_SSZK01000037.1.
DR AlphaFoldDB; P0AAG3; -.
DR SMR; P0AAG3; -.
DR BioGRID; 4259911; 22.
DR BioGRID; 849636; 1.
DR ComplexPortal; CPX-4324; Glutamate/aspartate ABC transporter complex.
DR DIP; DIP-48246N; -.
DR IntAct; P0AAG3; 6.
DR STRING; 511145.b0652; -.
DR TCDB; 3.A.1.3.4; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AAG3; -.
DR PaxDb; P0AAG3; -.
DR PRIDE; P0AAG3; -.
DR EnsemblBacteria; AAC73753; AAC73753; b0652.
DR EnsemblBacteria; BAA35304; BAA35304; BAA35304.
DR GeneID; 67416307; -.
DR GeneID; 945254; -.
DR KEGG; ecj:JW0647; -.
DR KEGG; eco:b0652; -.
DR PATRIC; fig|1411691.4.peg.1616; -.
DR EchoBASE; EB2529; -.
DR eggNOG; COG1126; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P0AAG3; -.
DR OMA; NWNQMRQ; -.
DR PhylomeDB; P0AAG3; -.
DR BioCyc; EcoCyc:GLTL-MON; -.
DR BioCyc; MetaCyc:GLTL-MON; -.
DR PRO; PR:P0AAG3; -.
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:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0015599; F:ATPase-coupled L-glutamine transmembrane transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IC:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR030679; ABC_ATPase_HisP-typ.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW Membrane; Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..241
FT /note="Glutamate/aspartate import ATP-binding protein GltL"
FT /id="PRO_0000092335"
FT DOMAIN 2..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 241 AA; 26661 MW; 7643584D63FC424D CRC64;
MITLKNVSKW YGHFQVLTDC STEVKKGEVV VVCGPSGSGK STLIKTVNGL EPVQQGEITV
DGIVVNDKKT DLAKLRSRVG MVFQHFELFP HLSIIENLTL AQVKVLKRDK APAREKALKL
LERVGLSAHA NKFPAQLSGG QQQRVAIARA LCMDPIAMLF DEPTSALDPE MINEVLDVMV
ELANEGMTMM VVTHEMGFAR KVANRVIFMD EGKIVEDSPK DAFFDDPKSD RAKDFLAKIL
H
