Y2550_BRUO2
ID Y2550_BRUO2 Reviewed; 302 AA.
AC A5VU89;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Putative peptide permease protein BOV_A0350;
GN OrderedLocusNames=BOV_A0350;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(2009).
CC -!- FUNCTION: Probably part of an ABC transporter complex that could be
CC involved in peptide import. Probably responsible for the translocation
CC of the substrate across the membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BOV_A0347
CC and BOV_A0348), two transmembrane proteins (BOV_A0350 and BOV_A0351)
CC and a solute-binding protein (BOV_A0352). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; CP000709; ABQ62079.1; -; Genomic_DNA.
DR AlphaFoldDB; A5VU89; -.
DR SMR; A5VU89; -.
DR EnsemblBacteria; ABQ62079; ABQ62079; BOV_A0350.
DR KEGG; bov:BOV_A0350; -.
DR HOGENOM; CLU_028518_1_1_5; -.
DR OMA; QDPTTYH; -.
DR Proteomes; UP000006383; Chromosome II.
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:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..302
FT /note="Putative peptide permease protein BOV_A0350"
FT /id="PRO_0000328712"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 200..222
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 97..288
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 32508 MW; A5DF3C86B43F4CA4 CRC64;
MRSSIHASRL RKMGQSIPAS TGPMARSANR FLQNRAAIFG LVLLTPLLFA VLTYPLWLPY
KPNDIDLMAM NSAPSWKHWF GADGVGRDVF ARTMEGGRIS LLVAVSSVVL STAIGFLIGA
ISALGGRWAD AIAMRSVDLA MTLPPVIFLL VLASIIGSGI WSTVVVIALL SWPVLSRMIR
ARLLELRERE FVMASRGMGA GLGHLLFRHG LPNSIDILVV YATLQVANAI LLEAGLSFLG
LGVPPPAASW GNMLNAARST AVLEQFPWQW LFPGGALVLA VLAINFIGDG LRDAFDPRAE
LN