THIT_LACLM
ID THIT_LACLM Reviewed; 182 AA.
AC A2RI47;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Thiamine transporter ThiT;
DE AltName: Full=Thiamine ECF transporter S component ThiT;
GN Name=thiT; OrderedLocusNames=llmg_0334;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, AND EXPRESSION IN E.COLI.
RC STRAIN=MG1363;
RX PubMed=21135102; DOI=10.1074/jbc.m110.199224;
RA ter Beek J., Duurkens R.H., Erkens G.B., Slotboom D.J.;
RT "Quaternary structure and functional unit of energy coupling factor (ECF)-
RT type transporters.";
RL J. Biol. Chem. 286:5471-5475(2011).
CC -!- FUNCTION: Probably a thiamine-binding protein that interacts with the
CC energy-coupling factor (ECF) ABC-transporter complex. Unlike classic
CC ABC transporters this ECF transporter provides the energy necessary to
CC transport a number of different substrates. The substrates themselves
CC are bound by transmembrane, not extracytoplasmic soluble proteins.
CC -!- SUBUNIT: In E.coli forms a stable energy-coupling factor (ECF)
CC transporter complex composed of 2 membrane-embedded substrate-binding
CC protein (S component), 2 ATP-binding proteins (A and A' components) and
CC 2 transmembrane proteins (T component), probably with a stoichiometry
CC of 2:1:1:2. May be able to interact with more than 1 S component at a
CC time. {ECO:0000269|PubMed:21135102}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21135102};
CC Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
CC -!- SIMILARITY: Belongs to the vitamin uptake transporter (VUT/ECF) (TC
CC 2.A.88) family. Thiamine transporter subfamily. {ECO:0000305}.
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DR EMBL; AM406671; CAL96940.1; -; Genomic_DNA.
DR RefSeq; WP_011834396.1; NZ_WJVF01000001.1.
DR PDB; 4POP; X-ray; 2.20 A; A/B=1-182.
DR PDB; 4POV; X-ray; 2.20 A; A/B=1-182.
DR PDBsum; 4POP; -.
DR PDBsum; 4POV; -.
DR AlphaFoldDB; A2RI47; -.
DR SMR; A2RI47; -.
DR STRING; 416870.llmg_0334; -.
DR BindingDB; A2RI47; -.
DR ChEMBL; CHEMBL4295631; -.
DR TCDB; 2.A.88.3.2; the vitamin uptake transporter (vut) family.
DR EnsemblBacteria; CAL96940; CAL96940; llmg_0334.
DR GeneID; 61108638; -.
DR KEGG; llm:llmg_0334; -.
DR eggNOG; COG3859; Bacteria.
DR HOGENOM; CLU_090959_2_0_9; -.
DR OMA; VQVLFDY; -.
DR PhylomeDB; A2RI47; -.
DR BioCyc; LLAC416870:LLMG_RS01725-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR012651; Thia_Transptr_ThiT.
DR Pfam; PF09515; Thia_YuaJ; 1.
DR TIGRFAMs; TIGR02357; ECF_ThiT_YuaJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..182
FT /note="Thiamine transporter ThiT"
FT /id="PRO_0000409009"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:4POP"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:4POP"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 107..132
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 143..172
FT /evidence="ECO:0007829|PDB:4POP"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:4POP"
SQ SEQUENCE 182 AA; 19909 MW; F5E4D6230BD8C8FB CRC64;
MSNSKFNVRL LTEIAFMAAL AFIISLIPNT VYGWIIVEIA CIPILLLSLR RGLTAGLVGG
LIWGILSMIT GHAYILSLSQ AFLEYLVAPV SLGIAGLFRQ KTAPLKLAPV LLGTFVAVLL
KYFFHFIAGI IFWSQYAWKG WGAVAYSLAV NGISGILTAI AAFVILIIFV KKFPKLFIHS
NY
