ID Q2YL39_BRUA2 Unreviewed; 537 AA.
AC Q2YL39;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Bacterial extracellular solute-binding protein, family 5 {ECO:0000313|EMBL:CAJ12617.1};
GN OrderedLocusNames=BAB2_0451 {ECO:0000313|EMBL:CAJ12617.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ12617.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ12617.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ12617.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000256|ARBA:ARBA00005695}.
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DR EMBL; AM040265; CAJ12617.1; -; Genomic_DNA.
DR RefSeq; WP_002965856.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YL39; -.
DR STRING; 359391.BAB2_0451; -.
DR GeneID; 3827160; -.
DR KEGG; bmf:BAB2_0451; -.
DR PATRIC; fig|359391.11.peg.2645; -.
DR HOGENOM; CLU_017028_7_3_5; -.
DR PhylomeDB; Q2YL39; -.
DR Proteomes; UP000002719; 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 CDD; cd08517; PBP2_NikA_DppA_OppA_like_13; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
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:SF38; D,D-DIPEPTIDE-BINDING PERIPLASMIC PROTEIN DDPA-RELATED; 1.
DR PANTHER; PTHR30290; PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004219145"
FT DOMAIN 83..434
FT /note="Solute-binding protein family 5"
FT /evidence="ECO:0000259|Pfam:PF00496"
SQ SEQUENCE 537 AA; 58633 MW; E3BBFC75672369AE CRC64;
MSGFVASRRA FLVGSTSLAA LAFWPKATWA AQEVQKGGRL VVAADSEPRN LNPAIIASNG
VFFVASKVIE PLAEAAYEGQ GGLAPRLATS WEGSADGLTA TFRLREGVNW HDGKPFTSAD
VAFSAMEVWK PLQNLGRVVF KSLEKVETPD EHTAIFHFSE PTPFQLIRNA LPALTAVLPK
HVFAGTDIAA NPANEKLAGT GPFKYAEHKT GEYYRLVKNA DYWGEGEPYL DEVIYRVLPD
RAAAADALEA GEIDLAAFSA VPLADLDRIS KVPGLAVISK GYEGLTYQLV VEINHRRKEL
ADLKVRQAIA HAIDRDFVVK TIFQGFAVPS TGPVPRYDSQ FYTDDVPTYP FDVKKANALL
DEAGYRRGKD GMRFALKLLP APYFNETKQF GDYLRQALAA IGIDAHIVNN DAAAHQKAVY
TDHDFDLAIA PTVYRGDPAI STTILVESGI PAGVPFSNQG GYANAELDAL IAKAASTTDE
KERTALYQKF QQMVEADLPL INVAEWGFIT VASERVKNVS NNPRWAVSNW ADTWLEP
//
