LYSP_ECOLI
ID LYSP_ECOLI Reviewed; 489 AA.
AC P25737; Q2MAS3;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Lysine-specific permease LysP {ECO:0000303|PubMed:1315732};
DE AltName: Full=Lysine transporter LysP {ECO:0000303|PubMed:24056175};
DE AltName: Full=Trigger transporter LysP {ECO:0000303|PubMed:24056175};
GN Name=lysP {ECO:0000303|PubMed:1315732}; Synonyms=cadR;
GN OrderedLocusNames=b2156, JW2143;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS A PERMEASE.
RC STRAIN=BPR2;
RX PubMed=1315732; DOI=10.1128/jb.174.10.3242-3249.1992;
RA Steffes C., Ellis J., Wu J., Rosen B.P.;
RT "The lysP gene encodes the lysine-specific permease.";
RL J. Bacteriol. 174:3242-3249(1992).
RN [2]
RP SEQUENCE REVISION.
RA Rosen B.P.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) 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 PROTEIN SEQUENCE OF 2-7, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=7551055; DOI=10.1099/13500872-141-8-1927;
RA Ellis J., Carlin A., Steffes C., Wu J., Liu J., Rosen B.P.;
RT "Topological analysis of the lysine-specific permease of Escherichia
RT coli.";
RL Microbiology 141:1927-1935(1995).
RN [7]
RP INDUCTION.
RX PubMed=8808945; DOI=10.1128/jb.178.18.5522-5528.1996;
RA Neely M.N., Olson E.R.;
RT "Kinetics of expression of the Escherichia coli cad operon as a function of
RT pH and lysine.";
RL J. Bacteriol. 178:5522-5528(1996).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
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 [9]
RP FUNCTION AS A LYSINE SENSOR, AND INTERACTION WITH CADC.
RX PubMed=18086202; DOI=10.1111/j.1365-2958.2007.06070.x;
RA Tetsch L., Koller C., Haneburger I., Jung K.;
RT "The membrane-integrated transcriptional activator CadC of Escherichia coli
RT senses lysine indirectly via the interaction with the lysine permease
RT LysP.";
RL Mol. Microbiol. 67:570-583(2008).
RN [10]
RP TRANSCRIPTIONAL REGULATION BY ARGP AND LRP.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21441513; DOI=10.1128/jb.00815-10;
RA Ruiz J., Haneburger I., Jung K.;
RT "Identification of ArgP and Lrp as transcriptional regulators of lysP, the
RT gene encoding the specific lysine permease of Escherichia coli.";
RL J. Bacteriol. 193:2536-2548(2011).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH CADC,
RP AND MUTAGENESIS OF TYR-102; TRP-106; LYS-163; PHE-216; GLU-222; GLU-230;
RP ASP-275; ASP-278; GLU-438; ASP-443 AND ASP-446.
RX PubMed=24056175; DOI=10.1016/j.jmb.2013.09.017;
RA Rauschmeier M., Schueppel V., Tetsch L., Jung K.;
RT "New insights into the interplay between the lysine transporter LysP and
RT the pH sensor CadC in Escherichia coli.";
RL J. Mol. Biol. 426:215-229(2014).
CC -!- FUNCTION: Permease involved in lysine uptake (PubMed:1315732,
CC PubMed:24056175). In addition, functions as a lysine sensor that
CC mediates the lysine-dependent regulation of the transcriptional
CC activator CadC (PubMed:18086202, PubMed:24056175). In the absence of
CC lysine, or at low lysine concentrations, LysP inhibits CadC by an
CC interaction with the transmembrane domain of CadC. In the presence of
CC lysine, LysP loses its ability to interact with and inhibit CadC, and
CC acts as a lysine permease (PubMed:18086202, PubMed:24056175).
CC {ECO:0000269|PubMed:1315732, ECO:0000269|PubMed:18086202,
CC ECO:0000269|PubMed:24056175}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-lysine(out) = H(+)(in) + L-lysine(in);
CC Xref=Rhea:RHEA:28911, ChEBI:CHEBI:15378, ChEBI:CHEBI:32551;
CC Evidence={ECO:0000305|PubMed:1315732, ECO:0000305|PubMed:24056175};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28912;
CC Evidence={ECO:0000305|PubMed:1315732, ECO:0000305|PubMed:24056175};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for lysine {ECO:0000269|PubMed:24056175};
CC Vmax=39.5 nmol/min/mg enzyme {ECO:0000269|PubMed:24056175};
CC -!- SUBUNIT: Interacts strongly with the transcriptional activator CadC in
CC the absence of lysine or at low lysine concentrations (PubMed:18086202,
CC PubMed:24056175). Interaction is markedly attenuated under increasing
CC lysine levels (PubMed:24056175). Concomitant pH-dependent protonation
CC of periplasmic amino acids in both proteins dissolves their
CC electrostatic connections resulting in further destabilization of the
CC CadC/LysP interaction (PubMed:24056175). Low pH promotes
CC oligomerization of LysP (PubMed:24056175).
CC {ECO:0000269|PubMed:18086202, ECO:0000269|PubMed:24056175}.
CC -!- INTERACTION:
CC P25737; P23890: cadC; NbExp=2; IntAct=EBI-6401655, EBI-6401662;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:7551055}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:7551055}.
CC -!- INDUCTION: Expression is repressed by high external lysine
CC concentrations (PubMed:8808945, PubMed:21441513). The HTH-type
CC transcriptional regulator ArgP is the main regulator of lysP
CC transcription (PubMed:21441513). Under lysine-limiting growth
CC conditions, ArgP functions as a transcriptional activator by binding
CC directly to the lysP promoter region (PubMed:21441513). In the presence
CC of lysine, Lys-loaded ArgP may prevent expression of the gene
CC (PubMed:21441513). In addition, expression is activated by the global
CC regulator Lrp under lysine-limiting conditions (PubMed:21441513).
CC Expression is not affected by pH (PubMed:8808945).
CC {ECO:0000269|PubMed:21441513, ECO:0000269|PubMed:8808945}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
CC {ECO:0000305}.
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DR EMBL; M89774; AAA17053.1; -; Genomic_DNA.
DR EMBL; U00007; AAA60532.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75217.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76633.1; -; Genomic_DNA.
DR PIR; C64984; C64984.
DR RefSeq; NP_416661.1; NC_000913.3.
DR RefSeq; WP_000253273.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P25737; -.
DR SMR; P25737; -.
DR BioGRID; 4260458; 13.
DR IntAct; P25737; 1.
DR STRING; 511145.b2156; -.
DR TCDB; 2.A.3.1.2; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P25737; -.
DR PRIDE; P25737; -.
DR EnsemblBacteria; AAC75217; AAC75217; b2156.
DR EnsemblBacteria; BAE76633; BAE76633; BAE76633.
DR GeneID; 66673948; -.
DR GeneID; 946667; -.
DR KEGG; ecj:JW2143; -.
DR KEGG; eco:b2156; -.
DR PATRIC; fig|1411691.4.peg.84; -.
DR EchoBASE; EB1313; -.
DR eggNOG; COG0833; Bacteria.
DR HOGENOM; CLU_007946_9_2_6; -.
DR InParanoid; P25737; -.
DR OMA; AMFSTAN; -.
DR PhylomeDB; P25737; -.
DR BioCyc; EcoCyc:LYSP-MON; -.
DR BioCyc; MetaCyc:LYSP-MON; -.
DR PRO; PR:P25737; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0097639; P:L-lysine import across plasma membrane; IMP:EcoCyc.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0043200; P:response to amino acid; IEP:EcoCyc.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7551055"
FT CHAIN 2..489
FT /note="Lysine-specific permease LysP"
FT /id="PRO_0000054204"
FT TOPO_DOM 2..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..45
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..128
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..197
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..290
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..370
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..446
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7551055"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:7551055"
FT SITE 275
FT /note="Essential for the stimulus-dependent interaction
FT with CadC"
FT /evidence="ECO:0000269|PubMed:24056175"
FT SITE 278
FT /note="Essential for the stimulus-dependent interaction
FT with CadC"
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 102
FT /note="Y->L: Retains 4% of wild-type lysine uptake
FT activity. Increases the capacity to inhibit CadC in the
FT presence of lysine."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 106
FT /note="W->L: Retains 20% of wild-type lysine uptake
FT activity. Increases the capacity to inhibit CadC in the
FT presence of lysine."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 163
FT /note="K->A: Retains 24% of wild-type lysine uptake
FT activity. Increases the capacity to inhibit CadC in the
FT presence of lysine."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 216
FT /note="F->L: Retains 13% of wild-type lysine uptake
FT activity. Increases the capacity to inhibit CadC in the
FT presence of lysine."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 222
FT /note="E->A: Abolishes lysine uptake. Strongly inhibits
FT CadC."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 230
FT /note="E->V: Abolishes lysine uptake. Shows significant
FT less inhibition of CadC."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 275
FT /note="D->A: Retains 88% of wild-type lysine uptake
FT activity, but can hardly inhibit CadC. Cannot interact with
FT CadC; when associated with A-278."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 278
FT /note="D->A: Retains 88% of wild-type lysine uptake
FT activity, but can hardly inhibit CadC. Cannot interact with
FT CadC; when associated with A-275."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 438
FT /note="E->A: Retains 14% of wild-type lysine uptake
FT activity. Is unable to inhibit CadC."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 443
FT /note="D->A: Retains 11% of wild-type lysine uptake
FT activity. Is unable to inhibit CadC."
FT /evidence="ECO:0000269|PubMed:24056175"
FT MUTAGEN 446
FT /note="D->A: Retains 13% of wild-type lysine uptake
FT activity. Is unable to inhibit CadC."
FT /evidence="ECO:0000269|PubMed:24056175"
FT CONFLICT 122
FT /note="S -> N (in Ref. 3; AAA60532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 53576 MW; 144FAFC01F2F8E7A CRC64;
MVSETKTTEA PGLRRELKAR HLTMIAIGGS IGTGLFVASG ATISQAGPGG ALLSYMLIGL
MVYFLMTSLG ELAAYMPVSG SFATYGQNYV EEGFGFALGW NYWYNWAVTI AVDLVAAQLV
MSWWFPDTPG WIWSALFLGV IFLLNYISVR GFGEAEYWFS LIKVTTVIVF IIVGVLMIIG
IFKGAQPAGW SNWTIGEAPF AGGFAAMIGV AMIVGFSFQG TELIGIAAGE SEDPAKNIPR
AVRQVFWRIL LFYVFAILII SLIIPYTDPS LLRNDVKDIS VSPFTLVFQH AGLLSAAAVM
NAVILTAVLS AGNSGMYAST RMLYTLACDG KAPRIFAKLS RGGVPRNALY ATTVIAGLCF
LTSMFGNQTV YLWLLNTSGM TGFIAWLGIA ISHYRFRRGY VLQGHDINDL PYRSGFFPLG
PIFAFILCLI ITLGQNYEAF LKDTIDWGGV AATYIGIPLF LIIWFGYKLI KGTHFVRYSE
MKFPQNDKK
