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 03-AUG-2022, entry version 111.
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}.
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DR EMBL; AE006468; AAL19071.1; -; Genomic_DNA.
DR RefSeq; NP_459112.1; NC_003197.2.
DR RefSeq; WP_000235634.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRV1; -.
DR SMR; Q8ZRV1; -.
DR STRING; 99287.STM0107; -.
DR PaxDb; Q8ZRV1; -.
DR EnsemblBacteria; AAL19071; AAL19071; STM0107.
DR GeneID; 1251625; -.
DR KEGG; stm:STM0107; -.
DR PATRIC; fig|99287.12.peg.110; -.
DR HOGENOM; CLU_021838_5_3_6; -.
DR OMA; PLYLFQL; -.
DR PhylomeDB; Q8ZRV1; -.
DR BioCyc; SENT99287:STM0107-MON; -.
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;
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
