GLTI_SALTY
ID GLTI_SALTY Reviewed; 302 AA.
AC Q9ZF60;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 3.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Glutamate/aspartate import solute-binding protein {ECO:0000250|UniProtKB:P37902};
DE Flags: Precursor;
GN Name=gltI; OrderedLocusNames=STM0665;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RC STRAIN=LEU485;
RA Gupta S.D., Rahman A., Wu H.C., Rick P.D.;
RT "Cloning and sequencing of apolipoprotein N-acyltransferase from Salmonella
RT typhimurium.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ABC transporter complex GltIJKL involved in
CC glutamate and aspartate uptake. Binds to both glutamate and aspartate.
CC {ECO:0000250|UniProtKB:P37902}.
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:P37902}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P37902}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09825.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL19616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL19616.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF116773; AAD09825.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_459657.1; NC_003197.2.
DR AlphaFoldDB; Q9ZF60; -.
DR SMR; Q9ZF60; -.
DR STRING; 99287.STM0665; -.
DR PaxDb; Q9ZF60; -.
DR EnsemblBacteria; AAL19616; AAL19616; STM0665.
DR GeneID; 1252185; -.
DR KEGG; stm:STM0665; -.
DR PATRIC; fig|99287.12.peg.701; -.
DR HOGENOM; CLU_019602_0_0_6; -.
DR OMA; PNQLDCL; -.
DR PhylomeDB; Q9ZF60; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P37902"
FT CHAIN 23..302
FT /note="Glutamate/aspartate import solute-binding protein"
FT /id="PRO_0000031759"
SQ SEQUENCE 302 AA; 33402 MW; AD0FD8A5797362CB CRC64;
MQLRKLTTAM LVMGLSAGLA HAEDGAPAAG STLDKIAKNG VIVVGHRESS VPFSYYDNQQ
KVVGYSQDYS NAIVEAVKKK LNKPDLQVKL IPITSQNRIP LLQNGTFDFE CGSTTNNLER
QKQAAFSDTI FVVGTRLLTK KGGDIKDFPD LKGKAVVVTS GTTSEILLHK LNEEQKMGMR
IISAKDHGDS FRTLESGRAV AFMMDDALLA GERAKAKKPD NWEIVGKPQS QEAYGCMLRK
NDPEFKKLMD DTIAQAQTSG EAEKWFDKWF KNPIPPKNLN MNFELSDEMK ALFKAPNDKA
LN