Y3094_BRUAB
ID Y3094_BRUAB Reviewed; 302 AA.
AC Q577J7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Putative peptide permease protein BruAb2_0794;
GN OrderedLocusNames=BruAb2_0794;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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
CC (BruAb2_0796 and BruAb2_0797), two transmembrane proteins (BruAb2_0794)
CC and a solute-binding protein (BruAb2_0792). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX76187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017224; AAX76187.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q577J7; -.
DR SMR; Q577J7; -.
DR EnsemblBacteria; AAX76187; AAX76187; BruAb2_0794.
DR KEGG; bmb:BruAb2_0794; -.
DR HOGENOM; CLU_028518_1_1_5; -.
DR Proteomes; UP000000540; 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 BruAb2_0794"
FT /id="PRO_0000328708"
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 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; 32568 MW; 9215403A0DCC8CAB CRC64;
MRSSIHASRL RKMGQSIPAS TGPMARSANR FLQNRAAIFG LVLLTPLLFA VLTYPLWLPY
KPNDIDLMAM NSAPSWKHWF GTDGVGRDVF ARTMEGGRIS LLVAVSSVVL STAIGFLIGA
ISALGGRWAD AIAMRSVDLA MTLPPVIFLL VLASIIGSGI WSTVVVIALL SWPVLSRMIR
ARLLELRERE FVMASRGMGA GLGHLLFRHG LPNSIDILVV YATLQVANAI LLEAGLSFLG
LGVPPPAASW SNMLNAARST AVLEQFPWQW LFPGGALVLA VLAINFIGDG LRDAFDPRAE
LN
