MCTP_RHIL3
ID MCTP_RHIL3 Reviewed; 491 AA.
AC Q1M7A2; Q8VM88;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Monocarboxylate transport permease protein {ECO:0000303|PubMed:12218032};
GN Name=mctP {ECO:0000303|PubMed:12218032};
GN OrderedLocusNames=pRL100404 {ECO:0000312|EMBL:CAK10630.1};
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OG Plasmid pRL10 {ECO:0000312|EMBL:CAK10630.1}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=3841;
RX PubMed=12218032; DOI=10.1128/jb.184.19.5436-5448.2002;
RA Hosie A.H., Allaway D., Poole P.S.;
RT "A monocarboxylate permease of Rhizobium leguminosarum is the first member
RT of a new subfamily of transporters.";
RL J. Bacteriol. 184:5436-5448(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
CC -!- FUNCTION: Low-affinity transporter of alanine and high-affinity
CC transporter of lactate and pyruvate. Can also transport other
CC monocarboxylates such as propionate, butyrate, alpha-hydroxybutyrate or
CC acetate. May be proton coupled. Required for optimal growth on alanine
CC or pyruvate and ammonia. {ECO:0000269|PubMed:12218032}.
CC -!- ACTIVITY REGULATION: Inhibited by CCCP, but is apparently not affected
CC by the concentration of sodium. {ECO:0000269|PubMed:12218032}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.56 mM for alanine {ECO:0000269|PubMed:12218032};
CC KM=4.4 uM for lactate {ECO:0000269|PubMed:12218032};
CC KM=3.8 uM for pyruvate {ECO:0000269|PubMed:12218032};
CC Vmax=122 nmol/min/mg enzyme with alanine as substrate
CC {ECO:0000269|PubMed:12218032};
CC Vmax=22.4 nmol/min/mg enzyme with lactate as substrate
CC {ECO:0000269|PubMed:12218032};
CC Vmax=9.8 nmol/min/mg enzyme with pyruvate as substrate
CC {ECO:0000269|PubMed:12218032};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Transcriptionally regulated by the two-component regulatory
CC system MctS/MctR. {ECO:0000269|PubMed:12218032}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; AJ421944; CAD19128.1; -; Genomic_DNA.
DR EMBL; AM236084; CAK10630.1; -; Genomic_DNA.
DR RefSeq; WP_011654429.1; NC_008381.1.
DR AlphaFoldDB; Q1M7A2; -.
DR SMR; Q1M7A2; -.
DR TCDB; 2.A.21.4.1; the solute:sodium symporter (sss) family.
DR EnsemblBacteria; CAK10630; CAK10630; pRL100404.
DR KEGG; rle:pRL100404; -.
DR HOGENOM; CLU_018808_15_0_5; -.
DR OMA; PYVMLQQ; -.
DR OrthoDB; 231452at2; -.
DR SABIO-RK; Q1M7A2; -.
DR Proteomes; UP000006575; Plasmid pRL10.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; 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 Amino-acid transport; Cell membrane; Membrane; Plasmid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..491
FT /note="Monocarboxylate transport permease protein"
FT /id="PRO_0000430566"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 324..325
FT /note="SG -> FR (in Ref. 1; CAD19128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 52099 MW; 11CAC4DA79C9DA6F CRC64;
MTTDINGTAL AVFIFFFVLV TVMGFVASRW RKPETLAHID EWGLGGRNFG TWITWFLVGG
DFYTAYTVIA VPALVYTVGA YGFFALPYTI VVYPFVFMVM PVLWKRAKDF GYVTAGDVVH
GQYGSRGLEL AVAATGVIAT MPYIALQLVG MTAVLKALGL HGELPLAIAF IVLALYTYSA
GLRAPALIAF VKDIMIYIVV IAAVALIPSK LGGYANVFAS ADAAFQAKGS GNLLLGGNQY
VAYATLALGS ALAAFMYPHT LTGIFASNSG KTIRKNAIML PAYTLLLGLL ALLGYMGHAA
NLKLDSANDV VPTLFKTLFS GWFSGFAFAA IAIGALVPAA VMSIGAANLF TRNFWKAYVD
PDVSDAGEAK VAKITSLVVK VGALLVIIFL PTQFALDLQL LGGIWILQTL PALVFGLYTN
WFRAPGLLAG WFVGFGGGTF LVWDAGWKPL HLISLGGEPF TVYTGLLALA ANIAVAVVVN
ALLPAKAPVR A
