ID D3P9T8_DEFDS Unreviewed; 269 AA.
AC D3P9T8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Amino acid ABC transporter, substrate-binding protein {ECO:0000313|EMBL:BAI81478.1};
GN OrderedLocusNames=DEFDS_2028 {ECO:0000313|EMBL:BAI81478.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI81478.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI81478.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000256|ARBA:ARBA00010333, ECO:0000256|RuleBase:RU003744}.
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; AP011529; BAI81478.1; -; Genomic_DNA.
DR RefSeq; WP_013008723.1; NC_013939.1.
DR AlphaFoldDB; D3P9T8; -.
DR STRING; 639282.DEFDS_2028; -.
DR KEGG; ddf:DEFDS_2028; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_2_0; -.
DR OMA; WTKQHPE; -.
DR OrthoDB; 9768183at2; -.
DR Proteomes; UP000001520; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR CDD; cd13629; PBP2_Dsm1740; 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:UP000001520};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003048873"
FT DOMAIN 39..262
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT DOMAIN 39..261
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
SQ SEQUENCE 269 AA; 30822 MW; 13CD1BA989D9E57F CRC64;
MRKFFVSLLV FLFAATFLYA ADNSLWEKST LNQILKRGEL RVGLESGYKP FEMTAKNGEI
IGFDVDLAKV MAKAMGVKLK IVNTAWDGII PALITDKFDI IMSGMTITQK RNLQVNFADP
YIIVGQTLLI HKKDAGKIKS YKDLNNPKYV IASKLGTTGY FAAKKYIPKA KVNAFETEAD
AFQDFINGKA DAFVYDLPLC AYYYSLYKDR VVFLDKPFTF EPLGWAIKKG DPDFLNWLNN
FLRQIKGDGT YDRIYKKWFK SKSWHKQVQ
//