Y2787_BRUAB
ID Y2787_BRUAB Reviewed; 350 AA.
AC Q578M5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative ATP-binding protein BruAb2_0487;
DE EC=7.-.-.-;
GN OrderedLocusNames=BruAb2_0487;
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. Probably
CC responsible for energy coupling to the transport system (Probable).
CC {ECO:0000305}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins
CC (BruAb2_0487), two transmembrane proteins (BruAb2_0483) and a solute-
CC binding protein (BruAb2_0484). {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; AAX75909.1; -; Genomic_DNA.
DR RefSeq; WP_002965898.1; NC_006933.1.
DR AlphaFoldDB; Q578M5; -.
DR SMR; Q578M5; -.
DR EnsemblBacteria; AAX75909; AAX75909; BruAb2_0487.
DR GeneID; 3827857; -.
DR KEGG; bmb:BruAb2_0487; -.
DR HOGENOM; CLU_000604_1_1_5; -.
DR OMA; PRNMYDK; -.
DR Proteomes; UP000000540; Chromosome II.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR CDD; cd03301; ABC_MalK_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
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; IPR015855; ABC_transpr_MalK-like.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Translocase; Transport.
FT CHAIN 1..350
FT /note="Putative ATP-binding protein BruAb2_0487"
FT /id="PRO_0000281200"
FT DOMAIN 4..234
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 350 AA; 37984 MW; A43F81FE5C1E44D1 CRC64;
MKEVSLRGIS KTFGQLTVLD RIDLEIHSGE FLVLVGPSGC GKSTLLRMVA GLEPISGGDL
VIGGERANEL PPQKRNIAMV FQSYALFPHM TARENIGFGP RIRGEKAAET AAKVDHAASI
LNLHSYLDRY PRQLSGGQRQ RVAMGRAIVR EPSVFLFDEP LSNLDAQLRV QMRTEIKALH
QRLKSTVIYV THDQIEAMTM ADRIVVMNQG KIQQIGAPLD LYDRPANKFV AGFIGSPSMS
FIPGTVADGF FCTGEGEKIA VSAAAKGARA AEAGIRPENF VIAREGAGLT LVVEVIEPTG
PETHIYGRIA GEPVRAVFRE RIQLAPGEQV PVTAGSEHIH LFDKESGLPL
