ID   MCTC_CORGL              Reviewed;         551 AA.
AC   Q8NS49; Q6M6V3;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Monocarboxylic acid transporter {ECO:0000303|PubMed:19028892};
GN   Name=mctC {ECO:0000303|PubMed:19028892};
GN   OrderedLocusNames=Cgl0833 {ECO:0000312|EMBL:BAB98226.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=19028892; DOI=10.1128/jb.01155-08;
RA   Jolkver E., Emer D., Ballan S., Kraemer R., Eikmanns B.J., Marin K.;
RT   "Identification and characterization of a bacterial transport system for
RT   the uptake of pyruvate, propionate, and acetate in Corynebacterium
RT   glutamicum.";
RL   J. Bacteriol. 191:940-948(2009).
CC   -!- FUNCTION: Acts as a secondary carrier for acetate, propionate and
CC       pyruvate. Has high affinity for acetate and propionate and lower
CC       affinity for pyruvate. Driven by the electrochemical proton potential.
CC       {ECO:0000269|PubMed:19028892}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=143 nmol/min/mg enzyme with acetate as substrate
CC         {ECO:0000269|PubMed:19028892};
CC         Vmax=14 nmol/min/mg enzyme with propionate as substrate
CC         {ECO:0000269|PubMed:19028892};
CC         Vmax=5.6 nmol/min/mg enzyme with pyruvate as substrate
CC         {ECO:0000269|PubMed:19028892};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Transcriptionally regulated by RamA and RamB.
CC       {ECO:0000269|PubMed:19028892}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000305}.
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DR   EMBL; BA000036; BAB98226.1; -; Genomic_DNA.
DR   RefSeq; NP_600062.1; NC_003450.3.
DR   RefSeq; WP_011013917.1; NC_006958.1.
DR   AlphaFoldDB; Q8NS49; -.
DR   SMR; Q8NS49; -.
DR   STRING; 196627.cg0953; -.
DR   TCDB; 2.A.21.7.3; the solute:sodium symporter (sss) family.
DR   PRIDE; Q8NS49; -.
DR   KEGG; cgl:Cgl0833; -.
DR   PATRIC; fig|196627.13.peg.817; -.
DR   eggNOG; COG4147; Bacteria.
DR   HOGENOM; CLU_018808_8_3_11; -.
DR   OMA; GTTWVQM; -.
DR   Proteomes; UP000000582; 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; 1.20.1730.10; -; 1.
DR   InterPro; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   Pfam; PF00474; SSF; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..551
FT                   /note="Monocarboxylic acid transporter"
FT                   /id="PRO_0000440952"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   551 AA;  57268 MW;  4CF7C7E12E5E374C CRC64;
     MNSTILLAQD AVSEGVGNPI LNISVFVVFI IVTMTVVLRV GKSTSESTDF YTGGASFSGT
     QNGLAIAGDY LSAASFLGIV GAISLNGYDG FLYSIGFFVA WLVALLLVAE PLRNVGRFTM
     ADVLSFRLRQ KPVRVAAACG TLAVTLFYLI AQMAGAGSLV SVLLDIHEFK WQAVVVGIVG
     IVMIAYVLLG GMKGTTYVQM IKAVLLVGGV AIMTVLTFVK VSGGLTTLLN DAVEKHAASD
     YAATKGYDPT QILEPGLQYG ATLTTQLDFI SLALALCLGT AGLPHVLMRF YTVPTAKEAR
     KSVTWAIVLI GAFYLMTLVL GYGAAALVGP DRVIAAPGAA NAAAPLLAFE LGGSIFMALI
     SAVAFATVLA VVAGLAITAS AAVGHDIYNA VIRNGQSTEA EQVRVSRITV VVIGLISIVL
     GILAMTQNVA FLVALAFAVA ASANLPTILY SLYWKKFNTT GAVAAIYTGL ISALLLIFLS
     PAVSGNDSAM VPGADWAIFP LKNPGLVSIP LAFIAGWIGT LVGKPDNMDD LAAEMEVRSL
     TGVGVEKAVD H