SERP2_LACLM
ID SERP2_LACLM Reviewed; 460 AA.
AC A2RI86;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DL-alanine permease SerP2 {ECO:0000305};
GN Name=serP2 {ECO:0000303|PubMed:23144255};
GN OrderedLocusNames=llmg_0375 {ECO:0000312|EMBL:CAL96980.1};
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.
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).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=MG1363;
RX PubMed=25535271; DOI=10.1128/jb.02471-14;
RA Noens E.E., Lolkema J.S.;
RT "Physiology and substrate specificity of two closely related amino acid
RT transporters, SerP1 and SerP2, of Lactococcus lactis.";
RL J. Bacteriol. 197:951-958(2015).
CC -!- FUNCTION: Transports DL-alanine, DL-serine and glycine
CC (PubMed:23144255, PubMed:25535271). The preferred substrate is DL-
CC alanine. L-serine is a low-affinity substrate (PubMed:25535271).
CC {ECO:0000269|PubMed:23144255, ECO:0000269|PubMed:25535271}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for L-alanine {ECO:0000269|PubMed:25535271};
CC KM=356 uM for L-serine {ECO:0000269|PubMed:25535271};
CC Vmax=115 nmol/min/mg enzyme with L-alanine as substrate
CC {ECO:0000269|PubMed:25535271};
CC Vmax=216 nmol/min/mg enzyme with L-serine as substrate
CC {ECO:0000269|PubMed:25535271};
CC Note=Not stereoselective. Affinities for the D- and L- isomers of
CC alanine and serine are in the same range.
CC {ECO:0000269|PubMed:25535271};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is only marginally affected in
CC medium that contains only free amino acids as a source of amino acids.
CC Mutant shows almost no change in serine and L-threonine uptake, but
CC shows a strong decrease in L-alanine uptake. SerP1/serP2 double mutant
CC is completely devoid of uptake activity of either L-serine, L-threonine
CC or L-alanine. {ECO:0000269|PubMed:25535271}.
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; CAL96980.1; -; Genomic_DNA.
DR RefSeq; WP_011675414.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RI86; -.
DR SMR; A2RI86; -.
DR STRING; 416870.llmg_0375; -.
DR EnsemblBacteria; CAL96980; CAL96980; llmg_0375.
DR KEGG; llm:llmg_0375; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_9; -.
DR OMA; VIMYLTP; -.
DR PhylomeDB; A2RI86; -.
DR BioCyc; LLAC416870:LLMG_RS01925-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 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 membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..460
FT /note="DL-alanine permease SerP2"
FT /id="PRO_0000442543"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 51523 MW; 9FB7B62C1B36EA5A CRC64;
MNTNQNDENI EKQPSQRGLK NRHIQLIAIA GTIGTGLFLG AGKSIHLTGP SIIFVYLIIG
ALMYILLRAI GEMLYQDPSQ HSFLNFVSRY MGAKPGYFIQ WSYLLVVVFV AMAELIAIGT
YINFWLPDLP IWMTEVFVLV LLTLLNTLNP KFFGETEFWF GMIKIVAIIG LILTAIILIF
SHYHTGTDTV SLTNITKGFE FFPNGVSSFF ESFQMVMFAF VSMEFIGMTA AETDNPRPTL
KKAINQIPIR IVLFYIGALL AIMSIYQWRD IPADKSPFVT IFQLIGIKWA AALVNFVVLT
SAASALNSAL FSITRNLYSL SQLNDDKILK PFTKFSKAGV PVNALLFTSL LILFTPFISM
IPAISNSFVF ITSVATNLFL VVYLMTLITY LKYRKSKDFD PSGFTLPAAH IFIPLAIAGF
VLIFISLFCF KDTIIPAIGS VIWVLIFGLF TFFRKIKTAD
