SFMCT_SYNFM
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 03-AUG-2022, entry version 73.
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; Proteobacteria; Deltaproteobacteria; 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}.
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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 EnsemblBacteria; ABK19037; ABK19037; Sfum_3364.
DR KEGG; sfu:Sfum_3364; -.
DR eggNOG; COG2223; Bacteria.
DR HOGENOM; CLU_001265_59_7_7; -.
DR OMA; AKWWQLA; -.
DR OrthoDB; 1594866at2; -.
DR Proteomes; UP000001784; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 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
