GLTI_ECOLI
ID GLTI_ECOLI Reviewed; 302 AA.
AC P37902; P41408; P77612; Q9R7T1; Q9R7T3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glutamate/aspartate import solute-binding protein {ECO:0000305};
DE Flags: Precursor;
GN Name=gltI; Synonyms=ybeJ, yzzK; OrderedLocusNames=b0655, JW5092;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-302.
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 [6]
RP PROTEIN SEQUENCE OF 23-33.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [8]
RP FUNCTION AS A GLUTAMATE-ASPARTATE BINDING PROTEIN, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=K12 / W3092;
RX PubMed=1091635; DOI=10.1016/s0021-9258(19)41639-6;
RA Willis R.C., Furlong C.E.;
RT "Purification and properties of a periplasmic glutamate-aspartate binding
RT protein from Escherichia coli K12 strain W3092.";
RL J. Biol. Chem. 250:2574-2580(1975).
RN [9]
RP FUNCTION.
RX PubMed=1091636; DOI=10.1016/s0021-9258(19)41640-2;
RA Willis R.C., Furlong C.E.;
RT "Interactions of a glutamate-aspartate binding protein with the glutamate
RT transport system of Escherichia coli.";
RL J. Biol. Chem. 250:2581-2586(1975).
RN [10]
RP FUNCTION.
RC STRAIN=D2W;
RX PubMed=336628; DOI=10.1016/s0021-9258(17)38344-8;
RA Schellenberg G.D., Furlong C.E.;
RT "Resolution of the multiplicity of the glutamate and aspartate transport
RT systems of Escherichia coli.";
RL J. Biol. Chem. 252:9055-9064(1977).
RN [11]
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. Binds to both glutamate and aspartate.
CC {ECO:0000269|PubMed:1091635, ECO:0000269|PubMed:1091636,
CC ECO:0000269|PubMed:336628, 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: Periplasm {ECO:0000269|PubMed:1091635}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; U82598; AAB40856.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73756.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35307.2; -; Genomic_DNA.
DR EMBL; U10981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64800; E64800.
DR RefSeq; NP_415188.1; NC_000913.3.
DR RefSeq; WP_001177086.1; NZ_SSZK01000037.1.
DR AlphaFoldDB; P37902; -.
DR SASBDB; P37902; -.
DR SMR; P37902; -.
DR BioGRID; 4260829; 18.
DR BioGRID; 851277; 2.
DR ComplexPortal; CPX-4324; Glutamate/aspartate ABC transporter complex.
DR DIP; DIP-11361N; -.
DR IntAct; P37902; 1.
DR STRING; 511145.b0655; -.
DR TCDB; 3.A.1.3.4; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P37902; -.
DR jPOST; P37902; -.
DR PaxDb; P37902; -.
DR PRIDE; P37902; -.
DR EnsemblBacteria; AAC73756; AAC73756; b0655.
DR EnsemblBacteria; BAA35307; BAA35307; BAA35307.
DR GeneID; 946938; -.
DR KEGG; ecj:JW5092; -.
DR KEGG; eco:b0655; -.
DR PATRIC; fig|1411691.4.peg.1613; -.
DR EchoBASE; EB2562; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_0_0_6; -.
DR InParanoid; P37902; -.
DR OMA; TANCARW; -.
DR PhylomeDB; P37902; -.
DR BioCyc; EcoCyc:G6359-MON; -.
DR BioCyc; MetaCyc:G6359-MON; -.
DR PRO; PR:P37902; -.
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:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0070335; F:aspartate binding; IPI:EcoCyc.
DR GO; GO:0016595; F:glutamate binding; IPI:EcoCyc.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; IDA:EcoCyc.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:EcoCyc.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Direct protein sequencing; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 23..302
FT /note="Glutamate/aspartate import solute-binding protein"
FT /id="PRO_0000031758"
SQ SEQUENCE 302 AA; 33420 MW; 6FFC3321040152EC CRC64;
MQLRKPATAI LALALSAGLA QADDAAPAAG STLDKIAKNG VIVVGHRESS VPFSYYDNQQ
KVVGYSQDYS NAIVEAVKKK LNKPDLQVKL IPITSQNRIP LLQNGTFDFE CGSTTNNVER
QKQAAFSDTI FVVGTRLLTK KGGDIKDFAN LKDKAVVVTS GTTSEVLLNK LNEEQKMNMR
IISAKDHGDS FRTLESGRAV AFMMDDALLA GERAKAKKPD NWEIVGKPQS QEAYGCMLRK
DDPQFKKLMD DTIAQVQTSG EAEKWFDKWF KNPIPPKNLN MNFELSDEMK ALFKEPNDKA
LN
