THRE_CORGT
ID THRE_CORGT Reviewed; 489 AA.
AC H7C6B6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Threonine/serine exporter {ECO:0000303|PubMed:11881894};
GN Name=thrE {ECO:0000303|PubMed:11514515};
GN ORFNames=APT58_12930 {ECO:0000312|EMBL:AMA01055.1},
GN AUO95_02805 {ECO:0000312|EMBL:OKX84828.1},
GN CS176_2351 {ECO:0000312|EMBL:GAV98121.1};
OS Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=1718;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A TRANSPORTER, ACTIVITY
RP REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14752;
RX PubMed=11514515; DOI=10.1128/JB.183.18.5317-5324.2001;
RA Simic P., Sahm H., Eggeling L.;
RT "L-threonine export: use of peptides to identify a new translocator from
RT Corynebacterium glutamicum.";
RL J. Bacteriol. 183:5317-5324(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS176;
RA Matsutani M., Trakulnaleamsai S., Yakushi T., Matsushita K.;
RT "Corynebacterium glutamicum CS176 whole genome sequencing project.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13870;
RA Yang J., Yang S.;
RT "Genome sequence of Corynebacterium glutamicum ATCC13870.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-56828;
RA Harhay G.P., Harhay D.M., Smith T.P.L., Bono J.L., Heaton M.P.,
RA Clawson M.L., Chitko-Mckown C.G., Capik S.F., DeDonder K.D., Apley M.D.,
RA Lubbers B.V., White B.J., Larson R.L.;
RT "Annotation of Corynebacterium glutamicum USDA-ARS-USMARC-56828.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP THRE FAMILY, AND PHYLOGENETIC ANALYSES.
RX PubMed=11881894; DOI=10.1016/s0923-2508(01)01281-5;
RA Yen M.R., Tseng Y.H., Simic P., Sahm H., Eggeling L., Saier M.H. Jr.;
RT "The ubiquitous ThrE family of putative transmembrane amino acid efflux
RT transporters.";
RL Res. Microbiol. 153:19-25(2002).
CC -!- FUNCTION: Catalyzes the export of L-threonine and L-serine from the
CC cell to the extracellular environment (PubMed:11514515). Export is
CC dependent on the proton motive force (PubMed:11514515).
CC {ECO:0000269|PubMed:11514515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-threonine(in) = H(+)(in) + L-threonine(out);
CC Xref=Rhea:RHEA:28995, ChEBI:CHEBI:15378, ChEBI:CHEBI:57926;
CC Evidence={ECO:0000305|PubMed:11514515};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28996;
CC Evidence={ECO:0000305|PubMed:11514515};
CC -!- ACTIVITY REGULATION: Transport is inhibited by the proton ionophore
CC carbonyl cyanide m-chlorophenylhydrazone (CCCP).
CC {ECO:0000269|PubMed:11514515}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows increased threonine peptide
CC sensitivity (PubMed:11514515). Mutant still exports L-threonine, but at
CC a reduced rate (PubMed:11514515). {ECO:0000269|PubMed:11514515}.
CC -!- SIMILARITY: Belongs to the ThrE exporter (TC 2.A.79) family.
CC {ECO:0000305|PubMed:11881894}.
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DR EMBL; AF326510; AAK61331.1; -; Genomic_DNA.
DR EMBL; CP013991; AMA01055.1; -; Genomic_DNA.
DR EMBL; BAYH01000035; GAV98121.1; -; Genomic_DNA.
DR EMBL; LOQV01000009; OKX84828.1; -; Genomic_DNA.
DR RefSeq; WP_003853939.1; NZ_LOQW01000007.1.
DR EnsemblBacteria; AMA01055; AMA01055; APT58_12930.
DR EnsemblBacteria; GAV98121; GAV98121; CS176_2351.
DR EnsemblBacteria; OKX84828; OKX84828; AUO95_02805.
DR GeneID; 58308931; -.
DR KEGG; cgj:AR0_12740; -.
DR PATRIC; fig|1718.43.peg.2596; -.
DR OMA; MLSCGTG; -.
DR Proteomes; UP000069326; Chromosome.
DR Proteomes; UP000186616; Unassembled WGS sequence.
DR Proteomes; UP000188825; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR010619; ThrE.
DR InterPro; IPR024528; ThrE_2.
DR Pfam; PF06738; ThrE; 1.
DR Pfam; PF12821; ThrE_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..489
FT /note="Threonine/serine exporter"
FT /id="PRO_5015093756"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 489 AA; 51698 MW; E6639A9A6BFE0175 CRC64;
MLSFATLRGR ISTVDAAKAA PPPSPLAPID LTDHSQVAGV MNLAARIGDI LLSSGTSNSD
TKVQVRAVTS AYGLYYTHVD ITLNTITIFT NIGVERKMPV NVFHVVGKLD TNFSKLSEVD
RLIRSIQAGA TPPEVAEKIL DELEQSPASY GFPVALLGWA MMGGAVAVLL GGGWQVSLIA
FITAFTIIAT TSFLGKKGLP TFFQNVVGGF IATLPASIAY SLALQFGLEI KPSQIIASGI
VVLLAGLTLV QSLQDGITGA PVTASARFFE TLLFTGGIVA GVGLGIQLSE ILHVMLPAME
SAAAPNYSST FARIIAGGVT AAAFAVGCYA EWSSVIIAGL TALMGSAFYY LFVVYLGPVS
AAAIAATAVG FTGGLLARRF LIPPLIVAIA GITPMLPGLA IYRGMYATLN DQTLMGFTNI
AVALATASSL AAGVVLGEWI ARRLRRPPRF NPYRAFTKAN EFSFQEEAEQ NQRRQRKRPK
TNQRFGNKR
