ID SFMCT_SYNFM Reviewed; 412 AA. AC A0LNN5; DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=L-lactate transporter {ECO:0000303|PubMed:31201333}; DE AltName: Full=SfMCT {ECO:0000303|PubMed:31201333}; GN OrderedLocusNames=Sfum_3364 {ECO:0000312|EMBL:ABK19037.1}; OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB). OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales; OC Syntrophobacteraceae; Syntrophobacter. OX NCBI_TaxID=335543; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10017 / MPOB; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.; RT "Complete sequence of Syntrophobacter fumaroxidans MPOB."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) IN COMPLEXES WITH THE RP MONOCARBOXYLATES THIOSALICYLATE AND L-LACTATE, FUNCTION, ACTIVITY RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY, RP AND MUTAGENESIS OF LEU-28; TYR-119; LEU-145; HIS-250; ARG-256; ASP-257; RP ASN-276; ARG-280; TYR-331; PHE-335; PHE-359; CYS-362; LYS-377; ASP-378 AND RP TYR-383. RX PubMed=31201333; DOI=10.1038/s41467-019-10566-6; RA Bosshart P.D., Kalbermatter D., Bonetti S., Fotiadis D.; RT "Mechanistic basis of L-lactate transport in the SLC16 solute carrier RT family."; RL Nat. Commun. 10:2649-2649(2019). CC -!- FUNCTION: Proton-coupled L-lactate specific transporter. CC {ECO:0000269|PubMed:31201333}. CC -!- ACTIVITY REGULATION: Inhibited by the protonophore carbonyl cyanide m- CC chlorophenylhydrazone (CCCP), but not by valinomycin. CC {ECO:0000269|PubMed:31201333}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=233 uM for L-lactate {ECO:0000269|PubMed:31201333}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:31201333}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000478; ABK19037.1; -; Genomic_DNA. DR RefSeq; WP_011700162.1; NC_008554.1. DR PDB; 6G9X; X-ray; 2.54 A; A/B=1-412. DR PDB; 6HCL; X-ray; 2.69 A; A/B=1-412. DR PDB; 6ZGR; X-ray; 2.46 A; A/B=1-412. DR PDB; 6ZGS; X-ray; 2.15 A; A/B=1-412. DR PDB; 6ZGT; X-ray; 2.23 A; A/B=1-412. DR PDB; 6ZGU; X-ray; 2.18 A; A/B=1-412. DR PDBsum; 6G9X; -. DR PDBsum; 6HCL; -. DR PDBsum; 6ZGR; -. DR PDBsum; 6ZGS; -. DR PDBsum; 6ZGT; -. DR PDBsum; 6ZGU; -. DR AlphaFoldDB; A0LNN5; -. DR SMR; A0LNN5; -. DR STRING; 335543.Sfum_3364; -. DR KEGG; sfu:Sfum_3364; -. DR eggNOG; COG2223; Bacteria. DR HOGENOM; CLU_001265_59_7_7; -. DR InParanoid; A0LNN5; -. DR OrthoDB; 146345at2; -. DR Proteomes; UP000001784; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR CDD; cd17353; MFS_OFA_like; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR11360:SF284; MFS DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR11360; MONOCARBOXYLATE TRANSPORTER; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..412 FT /note="L-lactate transporter" FT /id="PRO_0000448001" FT TOPO_DOM 1..10 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 11..40 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 41..45 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 46..74 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 75 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 76..95 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 96..99 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 100..129 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 130..133 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 134..160 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 161..167 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 168..187 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 188..227 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 228..257 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 258..261 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 262..290 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 291..292 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 293..313 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 314..316 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 317..346 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 347..350 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 351..380 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 381..382 FT /note="Periplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT TRANSMEM 383..403 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:31201333" FT TOPO_DOM 404..412 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:31201333" FT BINDING 119 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000269|PubMed:31201333" FT BINDING 280 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 28 FT /note="L->A: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 119 FT /note="Y->A,F: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 145 FT /note="L->A: Strong decrease in transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 250 FT /note="H->A: Strong decrease in transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 250 FT /note="H->F: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 256 FT /note="R->A: No change in transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 256 FT /note="R->D: Increases transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 257 FT /note="D->A: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 276 FT /note="N->A: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 280 FT /note="R->A: Abolishes L-lactate binding and L-lactate FT transport." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 331 FT /note="Y->A: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 331 FT /note="Y->F: No change in transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 335 FT /note="F->A: Increases transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 359 FT /note="F->A: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 362 FT /note="C->A: Decrease in transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 377 FT /note="K->A,D: No change in transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 378 FT /note="D->A: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 383 FT /note="Y->A: Loss of transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT MUTAGEN 383 FT /note="Y->F: Strong decrease in transport activity." FT /evidence="ECO:0000269|PubMed:31201333" FT HELIX 12..33 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 35..41 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 46..74 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 76..95 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 100..106 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 109..129 FT /evidence="ECO:0007829|PDB:6ZGS" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:6ZGR" FT HELIX 134..161 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 167..187 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 221..225 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 228..247 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 251..257 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 262..290 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 293..313 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 317..346 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 351..380 FT /evidence="ECO:0007829|PDB:6ZGS" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:6ZGS" FT HELIX 384..403 FT /evidence="ECO:0007829|PDB:6ZGS" SQ SEQUENCE 412 AA; 43800 MW; 139A0300465FDD45 CRC64; MADQQTTMPR WVPLLLGLLG STTCGMLLYA WSVFIKPLNA EFGWSRAEIA MAFAICCLIF GLMTFPAGRL SDKMGPRKVV MTGGVLLAIG FILSGFIQSK YQLYITYGVI AGFGGGMIYL PPIATAPKWW PDRRALATGF AVVGLGLGSF LMGPLATYII EKPGMGWRYV FWYCGVAMGI MALIAGAFLE PPPAGWKPAG YTPPAPPAGA AAPKVTRDWT YEEAKGDTKF WLLYLAYFCG SFAGLMVIGH LAGFGRDAGL TAMAAAGAVS SLAFSNAATR ILSGWFVDKI GIRVYFAALF ALQTAAMIAI FQLGGSVVGL SIVAIVIGWN YGAMFTLFPA TCLQFYGPTA QGSNYGLLFT ACGLAGFAGP WVGGWLKDTT GTYYLPFLCA AALCALGTAI VFMTKPPEKK HA //