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LARD_LACPL
ID   LARD_LACPL              Reviewed;         238 AA.
AC   F9UST3;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=D/L-lactic acid transporter {ECO:0000303|PubMed:23799297, ECO:0000303|PubMed:24710389};
DE   AltName: Full=Lactate racemization operon protein LarD {ECO:0000303|PubMed:24710389};
DE   AltName: Full=Lactic acid channel {ECO:0000303|PubMed:23799297};
GN   Name=larD {ECO:0000303|PubMed:24710389};
GN   Synonyms=glpF1 {ECO:0000303|PubMed:16166538, ECO:0000303|PubMed:23799297,
GN   ECO:0000312|EMBL:CCC77664.1};
GN   OrderedLocusNames=lp_0108 {ECO:0000312|EMBL:CCC77664.1};
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
RN   [3]
RP   INDUCTION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=16166538; DOI=10.1128/jb.187.19.6750-6761.2005;
RA   Goffin P., Deghorain M., Mainardi J.L., Tytgat I., Champomier-Verges M.C.,
RA   Kleerebezem M., Hols P.;
RT   "Lactate racemization as a rescue pathway for supplying D-lactate to the
RT   cell wall biosynthesis machinery in Lactobacillus plantarum.";
RL   J. Bacteriol. 187:6750-6761(2005).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=23799297; DOI=10.1042/bj20130388;
RA   Bienert G.P., Desguin B., Chaumont F., Hols P.;
RT   "Channel-mediated lactic acid transport: a novel function for
RT   aquaglyceroporins in bacteria.";
RL   Biochem. J. 454:559-570(2013).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=24710389; DOI=10.1038/ncomms4615;
RA   Desguin B., Goffin P., Viaene E., Kleerebezem M., Martin-Diaconescu V.,
RA   Maroney M.J., Declercq J.P., Soumillion P., Hols P.;
RT   "Lactate racemase is a nickel-dependent enzyme activated by a widespread
RT   maturation system.";
RL   Nat. Commun. 5:3615-3615(2014).
CC   -!- FUNCTION: Transporter that facilitates the transmembrane diffusion of
CC       D/L-lactic acid. Is involved in the cellular racemization of lactate
CC       and lactate metabolism. The transported molecule is indeed lactic acid
CC       and not the lactate anion, in agreement with the assumption that, with
CC       very few exceptions, MIPs (major intrinsic proteins) only facilitate
CC       the transport of uncharged solutes. Also facilitates urea and H(2)O(2)
CC       diffusion across membranes, but is not permeable to water, glycerol and
CC       dihydroxyacetone. {ECO:0000269|PubMed:23799297}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23799297};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Induced by L-lactate and repressed by D-lactate. Is thus
CC       regulated by the L-lactate/D-lactate ratio. Makes part of the lar
CC       operon (larABCDE). {ECO:0000269|PubMed:16166538}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a decreased lactate
CC       transport ability (PubMed:23799297). Deletion of this gene does not
CC       affect lactate racemase activity (PubMed:24710389).
CC       {ECO:0000269|PubMed:23799297, ECO:0000269|PubMed:24710389}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000305}.
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DR   EMBL; AL935263; CCC77664.1; -; Genomic_DNA.
DR   RefSeq; WP_003643656.1; NC_004567.2.
DR   RefSeq; YP_004888178.1; NC_004567.2.
DR   AlphaFoldDB; F9UST3; -.
DR   SMR; F9UST3; -.
DR   STRING; 220668.lp_0108; -.
DR   EnsemblBacteria; CCC77664; CCC77664; lp_0108.
DR   GeneID; 57026950; -.
DR   KEGG; lpl:lp_0108; -.
DR   PATRIC; fig|220668.9.peg.88; -.
DR   eggNOG; COG0580; Bacteria.
DR   HOGENOM; CLU_020019_9_2_9; -.
DR   OMA; VMMAVYI; -.
DR   PhylomeDB; F9UST3; -.
DR   BioCyc; LPLA220668:G1GW0-86-MON; -.
DR   Proteomes; UP000000432; 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:0015267; F:channel activity; IEA:InterPro.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR000425; MIP.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..238
FT                   /note="D/L-lactic acid transporter"
FT                   /id="PRO_0000441642"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           62..64
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000305|PubMed:23799297"
FT   MOTIF           185..187
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000305|PubMed:23799297"
SQ   SEQUENCE   238 AA;  25449 MW;  BD0119ABDCAF056D CRC64;
     MVHQLIAEFM GTALMIIFGV GVHCSSVLKG TKYRGSGHIF AITTWGFGIS VALFIFGNVC
     INPAMVLAQC LLGNIAWSLF IPYSVAEVLG GVVGSVIVWI MYADHFKAST DEISPITIRN
     LFCTAPAVRN LPRNFFVELF DTFIFISGIL AISEIKTPGI VPIGVGLLVW AIGMGLGGPT
     GFAMNLARDM GPRIAHAILP IANKADSDWQ YGIIVPGIAP FVGAAIAAWF MHGFFGIN
 
 
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