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Database: UniProt
Entry: G8PP46_PSEUV
LinkDB: G8PP46_PSEUV
Original site: G8PP46_PSEUV 
ID   G8PP46_PSEUV            Unreviewed;       255 AA.
AC   G8PP46;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Nopaline-binding periplasmic protein {ECO:0000313|EMBL:AEV37076.1};
GN   OrderedLocusNames=PSE_2568 {ECO:0000313|EMBL:AEV37076.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV37076.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV37076.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV37076.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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; CP003147; AEV37076.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8PP46; -.
DR   STRING; 911045.PSE_2568; -.
DR   KEGG; psf:PSE_2568; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_0_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
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:SF27; L-ARGININE-BINDING 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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..255
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003513139"
FT   DOMAIN          24..251
FT                   /note="Solute-binding protein family 3/N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00062"
FT   DOMAIN          24..250
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
SQ   SEQUENCE   255 AA;  27614 MW;  E78BB3664D9CE283 CRC64;
     MRLAAVAAIA LAAVSGAEAK EWTKVRMGTE GAYPPFNYTT ADGTLTGFDI EIGNALCEEL
     KLECTWVTQD WDGIIPGLVA GKYDTILASM SITPERMEKI SFSEKYYNTP PGIAVRKDSE
     LTEATPEGLK GVRLGAQGST THSQFAEEIL NGSDVALYPT SEEYKLDLEN GRVDAVVDDV
     MALEQWISSD KGSCCKILGT MQSVEEIHGK GAGIGVRKGD EDLAALFTKG IAALRANGKY
     KEINDKYFKF DVYGE
//
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