Y1033_BRUAB
ID Y1033_BRUAB Reviewed; 332 AA.
AC Q8VQK6; Q576M5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative peptide import ATP-binding protein BruAb2_1033;
DE EC=7.4.2.-;
GN OrderedLocusNames=BruAb2_1033;
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 [GENOMIC DNA].
RC STRAIN=544 / Biovar 1;
RA Bricker B.J.;
RT "Tn1953, a new element from Brucella abortus.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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_1033 and BruAb2_1034), two transmembrane proteins (BruAb2_1031
CC and BruAb2_1032) and a solute-binding protein (BruAb2_1030).
CC {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; AF454951; AAL59343.1; -; Genomic_DNA.
DR EMBL; AE017224; AAX76409.1; -; Genomic_DNA.
DR RefSeq; WP_002965564.1; NC_006933.1.
DR AlphaFoldDB; Q8VQK6; -.
DR SMR; Q8VQK6; -.
DR EnsemblBacteria; AAX76409; AAX76409; BruAb2_1033.
DR GeneID; 45054075; -.
DR KEGG; bmb:BruAb2_1033; -.
DR HOGENOM; CLU_000604_1_23_5; -.
DR OMA; LDPINTI; -.
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..332
FT /note="Putative peptide import ATP-binding protein
FT BruAb2_1033"
FT /id="PRO_0000290156"
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