LYSP_LACLM
ID LYSP_LACLM Reviewed; 508 AA.
AC A2RNZ6;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Lysine-specific permease LysP {ECO:0000305};
DE AltName: Full=Lysine transporter LysP {ECO:0000303|PubMed:23144255};
GN Name=lysP {ECO:0000303|PubMed:23144255};
GN OrderedLocusNames=llmg_2477 {ECO:0000312|EMBL:CAL99041.1};
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP FUNCTION IN LYSINE UPTAKE, AND DISRUPTION PHENOTYPE.
RC STRAIN=MG1363;
RX PubMed=23144255; DOI=10.1128/jb.01948-12;
RA Trip H., Mulder N.L., Lolkema J.S.;
RT "Cloning, expression, and functional characterization of secondary amino
RT acid transporters of Lactococcus lactis.";
RL J. Bacteriol. 195:340-350(2013).
CC -!- FUNCTION: Permease involved in lysine uptake.
CC {ECO:0000269|PubMed:23144255}.
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:23144255};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28912;
CC Evidence={ECO:0000305|PubMed:23144255};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes high-affinity
CC lysine uptake without affecting growth on free amino acids.
CC {ECO:0000269|PubMed:23144255}.
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; AM406671; CAL99041.1; -; Genomic_DNA.
DR AlphaFoldDB; A2RNZ6; -.
DR SMR; A2RNZ6; -.
DR STRING; 416870.llmg_2477; -.
DR EnsemblBacteria; CAL99041; CAL99041; llmg_2477.
DR KEGG; llm:llmg_2477; -.
DR eggNOG; COG0833; Bacteria.
DR HOGENOM; CLU_007946_9_2_9; -.
DR OMA; AMFSTAN; -.
DR PhylomeDB; A2RNZ6; -.
DR BioCyc; LLAC416870:LLMG_RS12445-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR Pfam; PF00324; AA_permease; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="Lysine-specific permease LysP"
FT /id="PRO_0000442541"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 508 AA; 54973 MW; 8779D3B496E2EAFB CRC64;
MRVSLSLTSR CRINFIRERI LENSSNSTTE TQVKRALKSR HVSMIALGGT IGTGLFLTSG
DVIHTAGPFG ALTAYVLIGA MVYFLMTSLG EMATYLPTSG SFSDYGTRYV DPAFGFALGW
NYWLNWAITV AVDLTAVALC IKFWLPDVPS WIFSLIALII VFSINALSVK TFGETEYWLS
AIKITVVVLF LIIGFLSIFG IMGGHIDVAK NLSVGNHGFV GGLGSFTTGG GILGVLLVAG
FSFQGTELLG ITAGEAENPE KSIPKAMNSI FWRILVFYIL SIFVMAAIIP FTDPHLVGGN
SAAQSPFTIV FERVGFSIAA SIMNAVVLTS VVSAANSGMY ASTRMLYSLA KDGGAPKIFS
KTSKNGIPFI ALLATTAVAL LTFLTSIYGV SFFTLLVSAS GLTGFIAWIG IAISHFRFRR
AYVAQGKDVK KLPYHAKLFP FGPILALIMT VLVTLGQDPM LLFGKTWVQG VVMYAAIPLF
FILYLGYKFK NKTKLIPLKD VDLSRHKD
