THIP_ECOLI
ID THIP_ECOLI Reviewed; 536 AA.
AC P31549; P75636;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Thiamine transport system permease protein ThiP;
GN Name=thiP; Synonyms=yabK; OrderedLocusNames=b0067, JW0066;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 511.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN THIAMINE TRANSPORT, AND ACTIVITY REGULATION.
RC STRAIN=K12 / KG33;
RX PubMed=12175925; DOI=10.1016/s0005-2736(02)00477-7;
RA Hollenbach A.D., Dickson K.A., Washabaugh M.W.;
RT "Thiamine transport in Escherichia coli: the mechanism of inhibition by the
RT sulfhydryl-specific modifier N-ethylmaleimide.";
RL Biochim. Biophys. Acta 1564:421-428(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC thiamine import (PubMed:12175925). Probably responsible for the
CC translocation of the substrate across the membrane (Probable).
CC {ECO:0000269|PubMed:12175925, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Transport is inhibited by the sulfhydryl-specific
CC modifier N-ethylmaleimide. {ECO:0000269|PubMed:12175925}.
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:0000250|UniProtKB:Q8ZRV1}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC73178.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96636.2; -; Genomic_DNA.
DR PIR; C64728; C64728.
DR RefSeq; NP_414609.1; NC_000913.3.
DR RefSeq; WP_000235721.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P31549; -.
DR SMR; P31549; -.
DR BioGRID; 4263358; 12.
DR BioGRID; 849186; 1.
DR ComplexPortal; CPX-4387; Thiamine ABC transporter complex.
DR DIP; DIP-10989N; -.
DR IntAct; P31549; 1.
DR STRING; 511145.b0067; -.
DR TCDB; 3.A.1.19.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P31549; -.
DR PRIDE; P31549; -.
DR EnsemblBacteria; AAC73178; AAC73178; b0067.
DR EnsemblBacteria; BAB96636; BAB96636; BAB96636.
DR GeneID; 944784; -.
DR KEGG; ecj:JW0066; -.
DR KEGG; eco:b0067; -.
DR PATRIC; fig|1411691.4.peg.2215; -.
DR EchoBASE; EB1533; -.
DR eggNOG; COG1178; Bacteria.
DR HOGENOM; CLU_021838_5_3_6; -.
DR InParanoid; P31549; -.
DR OMA; PLYLFQL; -.
DR PhylomeDB; P31549; -.
DR BioCyc; EcoCyc:SFUB-MON; -.
DR BioCyc; MetaCyc:SFUB-MON; -.
DR PRO; PR:P31549; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0071934; P:thiamine transmembrane transport; IC:ComplexPortal.
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_0000060230"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
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; 59533 MW; F6F559EDA92B8C2A CRC64;
MATRRQPLIP GWLIPGVSAT TLVVAVALAA FLALWWNAPQ DDWVAVWQDS YLWHVVRFSF
WQAFLSALLS VIPAIFLARA LYRRRFPGRL ALLRLCAMTL ILPVLVAVFG ILSVYGRQGW
LATLCQSLGL EWTFSPYGLQ GILLAHVFFN LPMASRLLLQ ALENIPGEQR QLAAQLGMRS
WHFFRFVEWP WLRRQIPPVA ALIFMLCFAS FATVLSLGGG PQATTIELAI YQALSYDYDP
ARAAMLALLQ MVCCLGLVLL SQRLSKAIAP GTTLLQGWRD PDDRLHSRIC DTVLIVLALL
LLLPPLLAVI VDGVNRQLPE VLAQPVLWQA LWTSLRIALA AGVLCVVLTM MLLWSSRELR
ARQKMLAGQV LEMSGMLILA MPGIVLATGF FLLLNNTIGL PQSADGIVIF TNALMAIPYA
LKVLENPMRD ITARYSMLCQ SLGIEGWSRL KVVELRALKR PLAQALAFAC VLSIGDFGVV
ALFGNDDFRT LPFYLYQQIG SYRSQDGAVT ALILLLLCFL LFTVIEKLPG RNVKTD
