ID   Y1094_BRUSU             Reviewed;         332 AA.
AC   Q8FUW8; G0KE98;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Putative peptide import ATP-binding protein BRA1094/BS1330_II1086;
DE            EC=7.4.2.-;
GN   OrderedLocusNames=BRA1094, BS1330_II1086;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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 (BRA1094),
CC       two transmembrane proteins (BRA1092 and BRA1093) and a solute-binding
CC       protein (BRA1090). {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014292; AAN34259.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM20536.1; -; Genomic_DNA.
DR   RefSeq; WP_002965564.1; NZ_KN046805.1.
DR   AlphaFoldDB; Q8FUW8; -.
DR   SMR; Q8FUW8; -.
DR   GeneID; 58777098; -.
DR   KEGG; bms:BRA1094; -.
DR   KEGG; bsi:BS1330_II1086; -.
DR   PATRIC; fig|204722.21.peg.2014; -.
DR   HOGENOM; CLU_000604_1_23_5; -.
DR   PhylomeDB; Q8FUW8; -.
DR   Proteomes; UP000007104; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd03257; ABC_NikE_OppD_transporters; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01727; oligo_HPY; 1.
DR   PANTHER; PTHR43297:SF6; DIPEPTIDE TRANSPORT ATP-BINDING PROTEIN DPPD; 1.
DR   PANTHER; PTHR43297; OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN APPD; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..332
FT                   /note="Putative peptide import ATP-binding protein
FT                   BRA1094/BS1330_II1086"
FT                   /id="PRO_0000290160"
FT   DOMAIN          11..261
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   332 AA;  36610 MW;  C67DF5FFDEEECAAE CRC64;
     MTISLKTAPL LEVSNLSVDF RTDGGWINAV DDVNFTLAPR ETLGLVGESG SGKSVTALSL
     LRLHDQRNSR LGGSVRYKGE DLFTLATSRL RQIRGHEIAM VFQDPIHTLN PVLTIGRQIE
     EGLRLHHGLQ GREARKRAIE LLDRVRIPDA ARRIDEYPHR MSGGQRQRVM IAIAIAGDPK
     ILIADEPTTA LDVTVQAQIM ELLRNLRDEL SMSVILISHD LGLVSEFADR AMVMYAGQPV
     ETGPIDKIFD EPLHPYTEGL LSAIPDLDDD LDRLPTIPGS IPEPSRRPPG CRFAPRCTFA
     QASCVKPQPI MSLTGGRASR CPPRLPTEEC VL
//