ID   THIP_BRUA2              Reviewed;         543 AA.
AC   Q2YLW7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Thiamine transport system permease protein ThiP;
GN   Name=thiP; OrderedLocusNames=BAB1_1771;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
CC   -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC       thiamine import. Probably responsible for the translocation of the
CC       substrate across the membrane. {ECO:0000250|UniProtKB:Q8ZRV1}.
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:0000250|UniProtKB:P31549}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. CysTW subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM040264; CAJ11727.1; -; Genomic_DNA.
DR   RefSeq; WP_002964842.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YLW7; -.
DR   SMR; Q2YLW7; -.
DR   STRING; 359391.BAB1_1771; -.
DR   EnsemblBacteria; CAJ11727; CAJ11727; BAB1_1771.
DR   GeneID; 3788983; -.
DR   KEGG; bmf:BAB1_1771; -.
DR   PATRIC; fig|359391.11.peg.282; -.
DR   HOGENOM; CLU_021838_5_3_5; -.
DR   OMA; PLYLFQL; -.
DR   PhylomeDB; Q2YLW7; -.
DR   Proteomes; UP000002719; Chromosome I.
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: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; 1.
DR   SUPFAM; SSF161098; SSF161098; 2.
DR   TIGRFAMs; TIGR01253; thiP; 1.
DR   PROSITE; PS50928; ABC_TM1; 2.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..543
FT                   /note="Thiamine transport system permease protein ThiP"
FT                   /id="PRO_0000282908"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          62..266
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          339..530
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   543 AA;  58302 MW;  8D87A2F048FA8C25 CRC64;
     MTATPARRTS LASPATKPVA GGLALAFLAT LAGGALLALA LEAGGGGFDA AANFDTYLWR
     VARFTIWQAV ASSLLSVLFA IPIARALYAE ARFPGRGLIL RLFALPLALP ALVAVLGVTS
     IYGRNGLIAH ISDMLGHPMQ PDIYGIAGIL IAHIFFNMPL AVRLLLAAYE SIPDDHWKLA
     AQLGMGSRAR FRLIEWPVIR RSLPGMIGLV FMLCVTSFTT VLTLGGGPRA TTLEVAIYQS
     LHFDFDPARA VALTFTQLAL TLLILLILRL TGRPSEEGFT QTATPRRYGS PRKTERLFNI
     IVIALGFLYV ALPIAGVVVS GLTADLVRLL SERIVWHAIA TSLALGFSAA LLAVFLSLAL
     VAAREATRNA RIANIFDTGA SLILVMPPIV IGAGWFILLR HFTDPFVMAP LMVVTVNAAM
     AMPFAVRLLR PAWDTAASRH NKLCSQLGIK GFNRLRLIDW PSIRRPCGMA FAFAMALSLG
     DLGTIALFGS DALVTLPYLL LQRMGSYRTF DAAGLALILG VLCLALMMIA DRAAASRKEA
     FLQ