ID A0A0P8A9F4_9RHOB Unreviewed; 274 AA.
AC A0A0P8A9F4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=ABC-type amino acid uptake system substrate-binding component {ECO:0000313|EMBL:KPP90782.1};
GN ORFNames=HLUCCA05_05055 {ECO:0000313|EMBL:KPP90782.1};
OS Roseibaca calidilacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseibaca.
OX NCBI_TaxID=1666912 {ECO:0000313|EMBL:KPP90782.1, ECO:0000313|Proteomes:UP000050413};
RN [1] {ECO:0000313|EMBL:KPP90782.1, ECO:0000313|Proteomes:UP000050413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-91 {ECO:0000313|EMBL:KPP90782.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP90782.1}.
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; LJSG01000016; KPP90782.1; -; Genomic_DNA.
DR RefSeq; WP_072247064.1; NZ_FBYC01000004.1.
DR AlphaFoldDB; A0A0P8A9F4; -.
DR STRING; 1666912.Ga0058931_3051; -.
DR PATRIC; fig|1666912.4.peg.2763; -.
DR OrthoDB; 9807134at2; -.
DR Proteomes; UP000050413; Unassembled WGS sequence.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..274
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030013280"
FT DOMAIN 40..264
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT DOMAIN 40..263
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
SQ SEQUENCE 274 AA; 29642 MW; F9ED387DC07C84D5 CRC64;
MTFPSLKTMT IAATMALGAV LSSAAQAQES VLDTIQERGT LTVGMSTFVP WAMRSTEGEL
IGFEIDVATK LAEDMGVEVE FVPTAWSGII PALLAGKFDV IIGGMSITPQ RNLTVNFTAP
YANSGNQLAA NVELTADFTD MSDFDDTSVN LVCRRGVVGC DVLAASFPRA NILQFDDNAQ
ALQEVLNGNA HAIIASAPEP AFWVEDNAGT IELAFGGEYL ARGNEAFALR KGDPDALNFF
SNWILVNQEN GWLEERHDYW FSGRKAWMDV VATE
//
