SERP1_LACLM
ID SERP1_LACLM Reviewed; 459 AA.
AC A2RI87;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Serine permease SerP1 {ECO:0000305};
GN Name=serP1 {ECO:0000303|PubMed:23144255};
GN OrderedLocusNames=llmg_0376 {ECO:0000312|EMBL:CAL96981.1};
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 L-serine, L-threonine and L-cysteine with high
CC affinity (PubMed:23144255, PubMed:25535271). Stereoselective, with a
CC strong preference for L-serine. Is the main L-serine transporter and is
CC responsible for optimal growth in media containing free amino acids as
CC the sole source of amino acids. Is also the main transporter for L-
CC threonine (PubMed:25535271). {ECO:0000269|PubMed:23144255,
CC ECO:0000269|PubMed:25535271}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for L-serine {ECO:0000269|PubMed:25535271};
CC KM=30 uM for L-threonine {ECO:0000269|PubMed:25535271};
CC Vmax=57 nmol/min/mg enzyme with L-serine as substrate
CC {ECO:0000269|PubMed:25535271};
CC Vmax=54 nmol/min/mg enzyme with L-threonine as substrate
CC {ECO:0000269|PubMed:25535271};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows a significant growth defect
CC in medium that contains only free amino acids as a source of amino
CC acids. Mutant shows a strong decrease in L-serine uptake and cannot
CC transport L-threonine. Can still transport L-alanine. SerP1/serP2
CC double mutant is completely devoid of uptake activity of either L-
CC serine, L-threonine 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; CAL96981.1; -; Genomic_DNA.
DR RefSeq; WP_011834429.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RI87; -.
DR SMR; A2RI87; -.
DR STRING; 416870.llmg_0376; -.
DR EnsemblBacteria; CAL96981; CAL96981; llmg_0376.
DR KEGG; llm:llmg_0376; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_9; -.
DR OMA; ASVVFDW; -.
DR PhylomeDB; A2RI87; -.
DR BioCyc; LLAC416870:LLMG_RS01930-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..459
FT /note="Serine permease SerP1"
FT /id="PRO_0000442542"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 459 AA; 51331 MW; A48D90FA5CB64312 CRC64;
MEDIQKNHEA QRGLQNRHIQ LIAIAGTIGT GLFLGAGKTI QMTGPSVIFA YILIGIAMFF
FLRTIGEMLY NDPSQHSFLN FVTKYSGIRT GYFTQWSYWL VIVFVCISEL TAIGTYIQFW
LPHLPLWLIE IVMLALLFGL NTLNSRFFGE TEFWFAMIKV AAILGMIVTA IILVASNFHY
TTVLSGKTVN DTASLNNIFD GFQLFPHGAW NFVGALQMVM FAFTSMEFIG MTAAETVNPK
KSLPKAINQI PVRILLFYVG ALLAIMAIFN WHYIPADKSP FVIVFQLIGI KWAAALINFV
VLTSAASALN SSLFSATRNM YSLAKQHDKG RLTAFTKLSK AGIPINALYM ATALSLLAPV
LTLIPQIKNA FNFAASCTTN LFLVVYFITL YTYWQYRKSD DYNPNGFLTP KPTIAVPFIA
IIFAIVFASL FFNADTFYPA LGAIVWTLIF GLYSHFKKI
