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Y1030_BRUAB
ID   Y1030_BRUAB             Reviewed;         514 AA.
AC   Q8VQK3;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Putative peptide-binding periplasmic protein BruAb2_1030;
DE   Flags: Precursor;
GN   OrderedLocusNames=BruAb2_1030;
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. {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: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000305}.
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DR   EMBL; AF454951; AAL59346.1; -; Genomic_DNA.
DR   EMBL; AE017224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q8VQK3; -.
DR   SMR; Q8VQK3; -.
DR   Proteomes; UP000000540; Chromosome II.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR030678; Peptide/Ni-bd.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR023765; SBP_5_CS.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 1.
DR   PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE   3: Inferred from homology;
KW   Periplasm; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..514
FT                   /note="Putative peptide-binding periplasmic protein
FT                   BruAb2_1030"
FT                   /id="PRO_0000290143"
FT   CONFLICT        288
FT                   /note="A -> D (in Ref. 1; AAL59346)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  57238 MW;  27D301FCDA9387B3 CRC64;
     MTIRTLFNAI LLSTTLLAAP SLAETPKEGG TLVYASNAGP GTLDPHMGNS LVELEIAHQI
     YEGLVTIDAN YNTATMLAES YVLSEDGKTL TFKLRKGVKF HDGSDMKSDD VLASFERYAK
     VSPNAKVLDI VDHYETPDDY TFVIHLKEVN AAFLDTLKSP VYPFSINPAE QKDKPARELD
     IIGTGPFKLG EWKRDSHLYL EKFADYVADK GKPASGYAGE KKVYVDKVRV NFLSETNSRV
     AAIQTGEAQV TTQLTADATK KLQNAPGVKP LEIIPFCQQY LIVNTQQAPT NNSAIRKALR
     TAVNAEDILV VSGEAATMDP SMSYPGGAYY SKENAEPYYN QNNPDEAAKM LADAGYKGEE
     LVLLTNSNYD YMRDNIVLLA EQLQAAGFKA RVEMTDWATN STAMQTGSGK WNVSTTSFCS
     NPLLGPQQWQ SVVYLFPQVK SDALMDTAYK KFFTSLKLED RRAAWLDIEK HILDEAYMIK
     ISNRASGRAY RPDDIGGYPE YYMNFFWNVW LKKQ
 
 
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