Y2551_BRUO2
ID Y2551_BRUO2 Reviewed; 319 AA.
AC A5VU90;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Putative peptide permease protein BOV_A0351;
GN OrderedLocusNames=BOV_A0351;
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; ABQ62416.1; -; Genomic_DNA.
DR RefSeq; WP_004681739.1; NC_009504.1.
DR AlphaFoldDB; A5VU90; -.
DR SMR; A5VU90; -.
DR EnsemblBacteria; ABQ62416; ABQ62416; BOV_A0351.
DR GeneID; 45125758; -.
DR KEGG; bov:BOV_A0351; -.
DR HOGENOM; CLU_036879_1_2_5; -.
DR OMA; AKDYPLM; -.
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; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 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..319
FT /note="Putative peptide permease protein BOV_A0351"
FT /id="PRO_0000328713"
FT TRANSMEM 9..29
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 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 98..305
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 319 AA; 34426 MW; D1AF00139E480FA4 CRC64;
MLRYCLHRLL IGLGMLLALT ILIFVLLQLT PGDPIDAYIN PNVAMTQAEM DALRAQLGLD
RPLPVQYLAW LGQAVQGNLG HSLQRFNETV SGLIASRIGP TLLLMAAGLA IAIVIGVTTG
IISAVRRNSF PDYSFSVLAL LGISSPAFLT ALLGLYVFSV RLKWAPSGGM LTPATDFSIP
DLLRHLALPA LVLSIGHAAL IMRYMRSSML ETLNQDYVRT ARAKGVREFW VVVKHTLRNA
MLPVVTLIGS TIGLAVGGAI FIESVFNWPG MGLLLINAVE TRDYPVIMGA TLVIGACVII
VNILTDLAYA VIDPRIKVT