APIBP_PARG4
ID APIBP_PARG4 Reviewed; 312 AA.
AC B1G898;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=D-apiose import binding protein {ECO:0000305};
DE AltName: Full=D-apiose binding SBP {ECO:0000303|PubMed:29867142};
DE Flags: Precursor;
GN ORFNames=BgramDRAFT_5566 {ECO:0000312|EMBL:EDT07597.1},
GN R8871_06335 {ECO:0000312|EMBL:CAB3737527.1};
OS Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 /
OS NCIMB 13744 / C4D1M).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=396598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia graminis
RT C4D1M.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M;
RA De Canck E.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND SUBSTRATE-BINDING.
RX PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA Andersen H.M., Almo S.C., Gerlt J.A.;
RT "Functional assignment of multiple catabolic pathways for D-apiose.";
RL Nat. Chem. Biol. 14:696-705(2018).
CC -!- FUNCTION: Part of an ABC transporter complex involved in D-apiose
CC import (Probable). Binds D-apiose, D-ribose and D-ribulose
CC (PubMed:29867142). {ECO:0000269|PubMed:29867142,
CC ECO:0000305|PubMed:29867142}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; ABLD01000025; EDT07597.1; -; Genomic_DNA.
DR EMBL; CADIKA010000024; CAB3737527.1; -; Genomic_DNA.
DR RefSeq; WP_006052135.1; NZ_CADIKA010000024.1.
DR AlphaFoldDB; B1G898; -.
DR SMR; B1G898; -.
DR EnsemblBacteria; EDT07597; EDT07597; BgramDRAFT_5566.
DR Proteomes; UP000005045; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW Periplasm; Signal; Sugar transport; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..312
FT /note="D-apiose import binding protein"
FT /id="PRO_5002764152"
FT BINDING 39
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 115..116
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 162..164
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 168
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 218
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 243
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 263
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
SQ SEQUENCE 312 AA; 33080 MW; 57A170A332F70052 CRC64;
MKASKRWVAL AAATLTLFTA TGTAQAANLI AIITPSHDNP FFKAEADTAN ARAKALGYDT
IVLVHDDDAN KQSNLVDTAI ARGAKAIILD NAGSEASISA VRKAKAAGIP SFLIDREINA
TGIAVSQIVS NNYQGAQLGG RAFVKALGEK GNYVELVGRE ADINAGIRSK GYHDVIDQFP
NMKMVERQSA NWSQTEAYRV METILQSHPD VKGVIAGNDT MAMGASAALK AAKRSDVIVV
GFDGSNDVRD AIMRNDIRAT VLQPAALAAT EAVEQADKYM KTGSTGKPEK QLINCSLITK
ANAGKLDMFA LR