ID   Y3096_BRUAB             Reviewed;         338 AA.
AC   Q577J5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative peptide import ATP-binding protein BruAb2_0796;
DE            EC=7.4.2.-;
GN   OrderedLocusNames=BruAb2_0796;
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 energy coupling to
CC       the transport system (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}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE017224; AAX76189.1; -; Genomic_DNA.
DR   RefSeq; WP_002967326.1; NC_006933.1.
DR   AlphaFoldDB; Q577J5; -.
DR   SMR; Q577J5; -.
DR   EnsemblBacteria; AAX76189; AAX76189; BruAb2_0796.
DR   GeneID; 3827087; -.
DR   KEGG; bmb:BruAb2_0796; -.
DR   HOGENOM; CLU_000604_1_23_5; -.
DR   OMA; PYHTIGK; -.
DR   Proteomes; UP000000540; Chromosome II.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport; Translocase;
KW   Transport.
FT   CHAIN           1..338
FT                   /note="Putative peptide import ATP-binding protein
FT                   BruAb2_0796"
FT                   /id="PRO_0000328693"
FT   DOMAIN          7..263
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   338 AA;  36751 MW;  2583B49DFECAE9C2 CRC64;
     MSRQPILDIE GLRTVFRTRA REIVAVNDVD IVVNPGETVA LVGESGSGKS VTSLSIMRLL
     ARKVGFIDAG SIILRGKSGQ TVDLAAIDEE AMRRIRGNDI GMVFQEPMTS LNPVYTIGDQ
     IGEPLRVHRG TSRREALEAA VELLDRVGIP DARRRAGQYP HELSGGMRQR ATIAMALICN
     PTFLIADEPT TALDVTIQAQ ILDLMQKLQS ESGMGMLFVT HNLGVVAEIA QRVVVMYAGR
     IVESGPVKEV FRNPRHPYTM GLLRSMPRLG DATEMKRRGE KLNTIPGMVP GLANLPSGCA
     FAPRCSFAVE ACHAAVPPLA SVNEHHGSRC IRWQEIAA