Y3863_BRUME
ID Y3863_BRUME Reviewed; 338 AA.
AC Q8YBN6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative peptide import ATP-binding protein BMEII0863;
DE EC=7.4.2.-;
GN OrderedLocusNames=BMEII0863;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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 (BMEII0863
CC and BMEII0864), two transmembrane proteins (BMEII0860 and BMEII0861)
CC and a solute-binding protein (BMEII0859). {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; AE008918; AAL54105.1; -; Genomic_DNA.
DR PIR; AF3617; AF3617.
DR RefSeq; WP_004681736.1; NZ_GG703779.1.
DR AlphaFoldDB; Q8YBN6; -.
DR SMR; Q8YBN6; -.
DR STRING; 224914.BMEII0863; -.
DR EnsemblBacteria; AAL54105; AAL54105; BMEII0863.
DR GeneID; 29595844; -.
DR KEGG; bme:BMEII0863; -.
DR PATRIC; fig|224914.52.peg.2499; -.
DR eggNOG; COG0444; Bacteria.
DR OMA; PYHTIGK; -.
DR PhylomeDB; Q8YBN6; -.
DR Proteomes; UP000000419; 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 BMEII0863"
FT /id="PRO_0000328697"
FT DOMAIN 10..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; 36715 MW; D2764C94E2835C79 CRC64;
MSRQPILDIK GLRTVFRTRA REIVAVNDVD IVVNPGETVA LVGESGSGKS VTSLSIMRLL
ARKVGFIDAG SIILRGKSGQ TVDLAAIDEE AMRRIRGNDI GMVFQEPMTS LNPVYTIGDQ
IGEPLRVHRG TSRREALEAA VELLDRVGIP DARRRAGQYP HELSGGMRQR ATIAMALICN
PTLLIADEPT TALDVTIQAQ ILDLMQKLQS ESGMGMLFVT HNLGVVAEIA QRVVVMYAGR
IVESGPVKEV FRNPRHPYTM GLLRSMPRLG DATEMKRRGE KLNTIPGMVP GLANLPSGCA
FAPRCSFAVE ACHAAVPPLA SVNKHHGSRC IRWQEIAA