THIP_BRUME
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 03-AUG-2022, entry version 115.
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; Proteobacteria; 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 STRING; 224914.BMEI0284; -.
DR EnsemblBacteria; AAL51465; AAL51465; BMEI0284.
DR GeneID; 29593038; -.
DR KEGG; bme:BMEI0284; -.
DR KEGG; bmel:DK63_1149; -.
DR PATRIC; fig|224914.52.peg.1213; -.
DR eggNOG; COG1178; Bacteria.
DR OMA; PLYLFQL; -.
DR PhylomeDB; Q8YJ03; -.
DR Proteomes; UP000000419; 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; 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
