ID H8H0D9_DEIGI Unreviewed; 321 AA.
AC H8H0D9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Twin-arginine translocation pathway signal {ECO:0000313|EMBL:AFD27191.1};
GN OrderedLocusNames=DGo_PA0305 {ECO:0000313|EMBL:AFD27191.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OG Plasmid P1 {ECO:0000313|EMBL:AFD27191.1,
OG ECO:0000313|Proteomes:UP000007575}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD27191.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD27191.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RC PLASMID=Plasmid P1 {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000256|ARBA:ARBA00007639}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002192; AFD27191.1; -; Genomic_DNA.
DR RefSeq; WP_014695709.1; NC_017805.1.
DR AlphaFoldDB; H8H0D9; -.
DR KEGG; dgo:DGo_PA0305; -.
DR PATRIC; fig|745776.4.peg.3339; -.
DR HOGENOM; CLU_037628_3_3_0; -.
DR OrthoDB; 6196975at2; -.
DR Proteomes; UP000007575; Plasmid P1.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProt.
DR CDD; cd20007; PBP1_ABC_sugar_binding-like; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR PANTHER; PTHR46847; D-ALLOSE-BINDING PERIPLASMIC PROTEIN-RELATED; 1.
DR PANTHER; PTHR46847:SF1; D-ALLOSE-BINDING PERIPLASMIC PROTEIN-RELATED; 1.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
PE 3: Inferred from homology;
KW Plasmid {ECO:0000313|EMBL:AFD27191.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..321
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003612099"
FT DOMAIN 34..288
FT /note="Periplasmic binding protein"
FT /evidence="ECO:0000259|Pfam:PF13407"
SQ SEQUENCE 321 AA; 33240 MW; 2885A47BC1C73472 CRC64;
MRQFITAGLS ALVLAASAHG AGAQSAASAK KYRIALILGT TTDNFYTSMQ CGAQEAAKRL
GDVELTIQGA PRWDATLQTP VVNAVTASGV QAIAIAVNDG RALYAPLKAA NDKGIKIVGV
DTRLTDSGFV VSNISSDNRA LGAEAARTLA KLMGEKGTAL IPPITPGITT VADRIQGFID
EMKANHKNIK IAYKGISEDA SAFSAAFAAN PDITGMFLIA NNEALVAAGA IRQLPASRRD
KISVVSFDAA PALVQALKSN QIQAIVAQKP AQMGALAVET ARKALMGQAV AKSQPTGGVG
LTQSNINQPA FAQYVYKSNC N
//
