ID   THIP_BRUME              Reviewed;         543 AA.
AC   Q8YJ03;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Thiamine transport system permease protein ThiP;
GN   Name=thiP; OrderedLocusNames=BMEI0284;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAL51465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL51465.1; ALT_INIT; Genomic_DNA.
DR   PIR; AF3287; AF3287.
DR   RefSeq; WP_005970857.1; NZ_GG703781.1.
DR   AlphaFoldDB; Q8YJ03; -.
DR   SMR; Q8YJ03; -.
DR   GeneID; 29593038; -.
DR   KEGG; bme:BMEI0284; -.
DR   KEGG; bmel:DK63_1149; -.
DR   PATRIC; fig|224914.52.peg.1213; -.
DR   eggNOG; COG1178; Bacteria.
DR   PhylomeDB; Q8YJ03; -.
DR   Proteomes; UP000000419; Chromosome I.
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; MetI-like; 2.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR005947; ThiP_ABC_transpt.
DR   NCBIfam; TIGR01253; thiP; 1.
DR   PANTHER; PTHR30183; MOLYBDENUM TRANSPORT SYSTEM PERMEASE PROTEIN MODB; 1.
DR   PANTHER; PTHR30183:SF9; THIAMINE TRANSPORT SYSTEM PERMEASE PROTEIN THIP; 1.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; MetI-like; 2.
DR   PROSITE; PS50928; ABC_TM1; 2.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..543
FT                   /note="Thiamine transport system permease protein ThiP"
FT                   /id="PRO_0000282909"
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;  58303 MW;  5FADDDB7893B96AA CRC64;
     MTATPARRTS LASPATKPVA GGLALAFLAT LAGGALLALA LEAGGGGFDA AANFDTYLWR
     VARFTIWQAV ASSLLSVLFA IPIARALYAE ARFPGRGLIL RLFAQPLALP ALVAVLGVTS
     IYGRNGLIAH ISDMLGHPMQ PDIYGIAGIL IAHIFFNMPL AVRLLLAAYE SIPDDHWKLA
     AQLGMGSRAR FRLIDWPVIR 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
//