GLTK_ECOLI
ID GLTK_ECOLI Reviewed; 224 AA.
AC P0AER5; P41075;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glutamate/aspartate import permease protein GltK {ECO:0000305};
GN Name=gltK; OrderedLocusNames=b0653, JW0648;
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 TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP RECEPTOR FOR CDI TOXIN ENTRY INTO TARGET CELL CYTOPLASM (MICROBIAL
RP INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=26305955; DOI=10.1073/pnas.1512124112;
RA Willett J.L., Gucinski G.C., Fatherree J.P., Low D.A., Hayes C.S.;
RT "Contact-dependent growth inhibition toxins exploit multiple independent
RT cell-entry pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11341-11346(2015).
RN [8]
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 the
CC translocation of the substrate across the membrane.
CC {ECO:0000305|PubMed:9593292}.
CC -!- FUNCTION: (Microbial infection) Probably transports the toxic C-
CC terminal region of CdiA from P.luminescens strain TTO1 across the inner
CC membrane to the cytoplasm, where CdiA has a toxic effect. Toxin
CC transport is strain-specific, mutations in this gene do not confer
CC resistance to several other tested CdiA toxins.
CC {ECO:0000269|PubMed:26305955}.
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
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Disruption confers resistance to cellular
CC contact-dependent growth inhibition (CDI) CdiA of P.luminescens strain
CC TTO1, but not to several other tested CdiA toxins.
CC {ECO:0000269|PubMed:26305955}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. HisMQ subfamily. {ECO:0000305}.
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DR EMBL; U10981; AAA60981.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40854.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73754.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35305.1; -; Genomic_DNA.
DR PIR; C64800; C64800.
DR RefSeq; NP_415186.1; NC_000913.3.
DR RefSeq; WP_000272824.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P0AER5; -.
DR SMR; P0AER5; -.
DR BioGRID; 4259913; 8.
DR ComplexPortal; CPX-4324; Glutamate/aspartate ABC transporter complex.
DR STRING; 511145.b0653; -.
DR TCDB; 3.A.1.3.4; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AER5; -.
DR PRIDE; P0AER5; -.
DR EnsemblBacteria; AAC73754; AAC73754; b0653.
DR EnsemblBacteria; BAA35305; BAA35305; BAA35305.
DR GeneID; 66671073; -.
DR GeneID; 947354; -.
DR KEGG; ecj:JW0648; -.
DR KEGG; eco:b0653; -.
DR PATRIC; fig|1411691.4.peg.1615; -.
DR EchoBASE; EB2528; -.
DR eggNOG; COG0765; Bacteria.
DR HOGENOM; CLU_019602_1_1_6; -.
DR InParanoid; P0AER5; -.
DR OMA; WQSMKLV; -.
DR PhylomeDB; P0AER5; -.
DR BioCyc; EcoCyc:GLTK-MON; -.
DR BioCyc; MetaCyc:GLTK-MON; -.
DR PRO; PR:P0AER5; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
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 GO; GO:1901998; P:toxin transport; IMP:EcoCyc.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR043429; ArtM/GltK/GlnP/TcyL/YhdX-like.
DR InterPro; IPR030205; GltK/AatM.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR30614; PTHR30614; 1.
DR PANTHER; PTHR30614:SF1; PTHR30614:SF1; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..224
FT /note="Glutamate/aspartate import permease protein GltK"
FT /id="PRO_0000060037"
FT TOPO_DOM 1..19
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..94
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..196
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 20..216
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 224 AA; 24915 MW; 01BCB38D387807B6 CRC64;
MYEFDWSSIV PSLPYLLDGL VITLKITVTA VVIGILWGTM LAVMRLSSFA PVAWFAKAYV
NVFRSIPLVM VLLWFYLIVP GFLQNVLGLS PKNDIRLISA MVAFSMFEAA YYSEIIRAGI
QSISRGQSSA ALALGMTHWQ SMKLIILPQA FRAMVPLLLT QGIVLFQDTS LVYVLSLADF
FRTASTIGER DGTQVEMILF AGFVYFVISL SASLLVSYLK RRTA
