ID A5UU90_ROSS1 Unreviewed; 288 AA.
AC A5UU90;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Extracellular solute-binding protein, family 3 {ECO:0000313|EMBL:ABQ90193.1};
GN OrderedLocusNames=RoseRS_1803 {ECO:0000313|EMBL:ABQ90193.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ90193.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) 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; CP000686; ABQ90193.1; -; Genomic_DNA.
DR RefSeq; WP_011956540.1; NC_009523.1.
DR AlphaFoldDB; A5UU90; -.
DR STRING; 357808.RoseRS_1803; -.
DR KEGG; rrs:RoseRS_1803; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_2_0; -.
DR OrthoDB; 9774451at2; -.
DR Proteomes; UP000006554; 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:SF19; ABC TRANSPORTER ARGININE-BINDING PROTEIN ARTJ-RELATED; 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; PS51257; PROKAR_LIPOPROTEIN; 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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..288
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002688024"
FT DOMAIN 62..288
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT DOMAIN 62..285
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT REGION 25..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 30500 MW; B363D0D23DC69A1E CRC64;
MQKQTLIMLA FIAASLVMSA CGGAPAAQPT QPAAQPTQPT AQPTQPAAQT DGKLAQIRAA
GKLIVGTSAD YPPYESIDEN GNFVGFDMDL IRAVGEKLGV EVEIRDMPFD SLIASLQEGK
IDAVIAAMQA TAEREEKVDF TIPYRMTKDA FIGAGNTTIT LNKPEDAAGL TIGAQTGTVQ
EGWIQKNLVA TGLTPADKVF SYERADQAAL DLASGRLQLV LMDAEPALEL AKQNGLKVLL
ITEETAEGGK SIAIPEGASD LKAELDRIIQ QLIDDGTVKQ LQDKHGLP
//
