THIT_BACSU
ID THIT_BACSU Reviewed; 192 AA.
AC O32074;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Thiamine transporter ThiT;
DE AltName: Full=Thiamine ECF transporter S component ThiT;
GN Name=thiT; Synonyms=yuaJ; OrderedLocusNames=BSU30990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP IDENTIFICATION, AND PRELIMINARY FUNCTION.
RX PubMed=12376536; DOI=10.1074/jbc.m208965200;
RA Rodionov D.A., Vitreschak A.G., Mironov A.A., Gelfand M.S.;
RT "Comparative genomics of thiamin biosynthesis in procaryotes. New genes and
RT regulatory mechanisms.";
RL J. Biol. Chem. 277:48949-48959(2002).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN THIAMINE TRANSPORT.
RX PubMed=16291685; DOI=10.1128/jb.187.23.8127-8136.2005;
RA Schyns G., Potot S., Geng Y., Barbosa T.M., Henriques A., Perkins J.B.;
RT "Isolation and characterization of new thiamine-deregulated mutants of
RT Bacillus subtilis.";
RL J. Bacteriol. 187:8127-8136(2005).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16291685}.
CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC complex composed of a membrane-embedded substrate-binding protein (S
CC component), two ATP-binding proteins (A components) and a transmembrane
CC protein (T component). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells display deregulation of thiamine
CC biosynthesis and impaired export of thiamine products from the cell.
CC {ECO:0000269|PubMed:16291685}.
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; AL009126; CAB15077.1; -; Genomic_DNA.
DR PIR; C70006; C70006.
DR RefSeq; NP_390977.1; NC_000964.3.
DR RefSeq; WP_003228966.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32074; -.
DR SMR; O32074; -.
DR STRING; 224308.BSU30990; -.
DR TCDB; 2.A.88.3.1; the vitamin uptake transporter (vut) family.
DR PaxDb; O32074; -.
DR PRIDE; O32074; -.
DR EnsemblBacteria; CAB15077; CAB15077; BSU_30990.
DR GeneID; 937137; -.
DR KEGG; bsu:BSU30990; -.
DR PATRIC; fig|224308.179.peg.3359; -.
DR eggNOG; COG3859; Bacteria.
DR OMA; VQVLFDY; -.
DR PhylomeDB; O32074; -.
DR BioCyc; BSUB:BSU30990-MON; -.
DR Proteomes; UP000001570; 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: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 Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..192
FT /note="Thiamine transporter ThiT"
FT /id="PRO_0000360177"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 192 AA; 20452 MW; 644EAC416E3A4980 CRC64;
MNQSKQLVRL IEIAIMTAAA VILDIVSGMF LSMPQGGSVS IMMIPIFLIS FRWGVKAGLT
TGLLTGLVQI AIGNLFAQHP VQLLLDYIVA FAAIGISGCF ASSVRKAAVS KTKGKLIVSV
VSAVFIGSLL RYAAHVISGA VFFGSFAPKG TPVWIYSLTY NATYMVPSFI ICAIVLCLLF
MTAPRLLKSD KA
