(data stored in SCRATCH zone)

SWISSPROT: THIP_SALTY

ID   THIP_SALTY              Reviewed;         536 AA.
AC   Q8ZRV1;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=Thiamine transport system permease protein ThiP {ECO:0000305};
GN   Name=thiP {ECO:0000303|PubMed:9535878};
GN   Synonyms=yabK {ECO:0000312|EMBL:AAL19071.1};
GN   OrderedLocusNames=STM0107 {ECO:0000312|EMBL:AAL19071.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION IN THIAMINE AND THIAMINE PYROPHOSPHATE TRANSPORT, SUBUNIT,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=9535878; DOI=10.1074/jbc.273.15.8946;
RA   Webb E., Claas K., Downs D.;
RT   "thiBPQ encodes an ABC transporter required for transport of thiamine and
RT   thiamine pyrophosphate in Salmonella typhimurium.";
RL   J. Biol. Chem. 273:8946-8950(1998).
CC   -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC       thiamine import (PubMed:9535878). Probably responsible for the
CC       translocation of the substrate across the membrane (Probable). Is also
CC       involved in thiamine pyrophosphate transport (PubMed:9535878).
CC       {ECO:0000269|PubMed:9535878, ECO:0000305|PubMed:9535878}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ThiQ),
CC       two transmembrane proteins (ThiP) and a solute-binding protein (ThiB).
CC       {ECO:0000305|PubMed:9535878}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P31549}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Expression is repressed by thiamine.
CC       {ECO:0000269|PubMed:9535878}.
CC   -!- DISRUPTION PHENOTYPE: Insertions in thiBPQ cause a defect in the
CC       transport of both thiamine and TPP. {ECO:0000269|PubMed:9535878}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
DR   EMBL; AE006468; AAL19071.1; -; Genomic_DNA.
DR   RefSeq; NP_459112.1; NC_003197.2.
DR   RefSeq; WP_000235634.1; NC_003197.2.
DR   PaxDb; Q8ZRV1; -.
DR   EnsemblBacteria; AAL19071; AAL19071; STM0107.
DR   GeneID; 1251625; -.
DR   KEGG; stm:STM0107; -.
DR   PATRIC; fig|99287.12.peg.110; -.
DR   eggNOG; ENOG4106SMU; Bacteria.
DR   eggNOG; COG1178; LUCA.
DR   HOGENOM; HOG000272487; -.
DR   KO; K02063; -.
DR   OMA; SYLWHVI; -.
DR   PhylomeDB; Q8ZRV1; -.
DR   BioCyc; SENT99287:STM0107-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015888; P:thiamine transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 2.
DR   Gene3D; 1.10.3720.10; -; 2.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR005947; ThiP_ABC_transpt.
DR   Pfam; PF00528; BPD_transp_1; 2.
DR   SUPFAM; SSF161098; SSF161098; 2.
DR   TIGRFAMs; TIGR01253; thiP; 1.
DR   PROSITE; PS50928; ABC_TM1; 2.
PE   1: Evidence at protein level;
DR   PRODOM; Q8ZRV1.
DR   SWISS-2DPAGE; Q8ZRV1.
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..536
FT                   /note="Thiamine transport system permease protein ThiP"
FT                   /id="PRO_0000448617"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          56..261
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          331..525
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   536 AA;  59407 MW;  7D349CE36B6BC6E6 CRC64;
     MATRRQPLIP GWLIPGLCAA ALMITVSLAA FLALWLNAPS GAWSTIWRDS YLWHVVRFSF
     WQAFLSAVLS VVPAVFLARA LYRRRFPGRL ALLRLCAMTL ILPVLVAVFG ILSVYGRQGW
     LASLWQMLGL QWTFSPYGLQ GILLAHVFFN LPMASRLLLQ SLESIPGEQR QLAAQLGMRG
     WHFFRFVEWP WLRRQIPPVA ALIFMLCFAS FATVLSLGGG PQATTIELAI FQALSYDYDP
     ARAAMLALIQ MVCCLALVLL SQRLSKAIAP GMTLTQGWRD PDDRLHSRLT DALLIVLALL
     LLLPPLVAVV VDGVNRSLPE VLAQPILWQA VWTSLRIALA AGVLCVVLTM MLLWSSRELR
     QRQQLFAGQT LELSGMLILA MPGIVLATGF FLLLNNSVGL PESADGIVIF TNALMAIPYA
     LKVLENPMRD ITARYGMLCQ SLGIEGWSRL KIVELRALKR PLAQALAFAC VLSIGDFGVV
     ALFGNDNFRT LPFYLYQQIG SYRSQDGAVT ALILLLLCFT LFTLIEKLPG RHAKTD
//

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