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Database: UniProt
Entry: D6Y3N1_THEBD
LinkDB: D6Y3N1_THEBD
Original site: D6Y3N1_THEBD 
ID   D6Y3N1_THEBD            Unreviewed;       282 AA.
AC   D6Y3N1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Extracellular solute-binding protein family 3 {ECO:0000313|EMBL:ADG87060.1};
GN   OrderedLocusNames=Tbis_0329 {ECO:0000313|EMBL:ADG87060.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS   10125 / KCTC 9307 / NBRC 14880 / R51).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG87060.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG87060.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC   NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000256|ARBA:ARBA00010333, ECO:0000256|RuleBase:RU003744}.
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DR   EMBL; CP001874; ADG87060.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6Y3N1; -.
DR   STRING; 469371.Tbis_0329; -.
DR   KEGG; tbi:Tbis_0329; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_2_11; -.
DR   Proteomes; UP000006640; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   CDD; cd13530; PBP2_peptides_like; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR018313; SBP_3_CS.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR35936:SF17; GLUTAMINE-BINDING PERIPLASMIC PROTEIN; 1.
DR   PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006640};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..282
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003090833"
FT   DOMAIN          55..277
FT                   /note="Solute-binding protein family 3/N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00062"
FT   DOMAIN          55..276
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
SQ   SEQUENCE   282 AA;  29638 MW;  39799F287008141D CRC64;
     MAPWSTYRRV AGIGATALIT ALMVAACGGG GDTTASSPSE AASAAGGVKL VNPGKLTTCT
     NIPYEPFQFQ QGDKIVGFDV DIVDLVANKL GVQQEIVDID FAAIKSGAAL NAGKCDVAAA
     GMTITEERKQ NLDFSVPYFD ASQALMAKKG SGVTSLDDVK AKGLKLGAQA STTGLDYVKS
     QGFEPIEFAD SQKQLNGLQA GRVDVIVQDL PVVLTWLKKP EISAEYEMVG SLDTGEQYGI
     GLKKGNTELL NVVNEVINQA KADGTYATIY KKWFGTEPPS NS
//
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