GLTL_ECO57
ID GLTL_ECO57 Reviewed; 241 AA.
AC P0AAG4; P41076;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glutamate/aspartate import ATP-binding protein GltL {ECO:0000250|UniProtKB:P0AAG3};
DE EC=7.4.2.1 {ECO:0000250|UniProtKB:P0AAG3};
GN Name=gltL; OrderedLocusNames=Z0802, ECs0691;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:0000250|UniProtKB:P0AAG3}.
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:0000250|UniProtKB:P0AAG3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14674;
CC Evidence={ECO:0000250|UniProtKB:P0AAG3};
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:0000250|UniProtKB:P0AAG3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29036;
CC Evidence={ECO:0000250|UniProtKB:P0AAG3};
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:0000250|UniProtKB:P0AAG3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29040;
CC Evidence={ECO:0000250|UniProtKB:P0AAG3};
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:0000250|UniProtKB:P0AAG3}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AAG3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0AAG3}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG54986.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34114.1; -; Genomic_DNA.
DR PIR; C90715; C90715.
DR PIR; F85565; F85565.
DR RefSeq; NP_308718.1; NC_002695.1.
DR RefSeq; WP_000631384.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AAG4; -.
DR SMR; P0AAG4; -.
DR STRING; 155864.EDL933_0729; -.
DR EnsemblBacteria; AAG54986; AAG54986; Z0802.
DR EnsemblBacteria; BAB34114; BAB34114; ECs_0691.
DR GeneID; 67416307; -.
DR GeneID; 917052; -.
DR KEGG; ece:Z0802; -.
DR KEGG; ecs:ECs_0691; -.
DR PATRIC; fig|386585.9.peg.805; -.
DR eggNOG; COG1126; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; NWNQMRQ; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015599; F:ATPase-coupled L-glutamine transmembrane transporter activity; IEA:UniProtKB-EC.
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_0000092336"
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
