ID   APIBP_AGRRK             Reviewed;         313 AA.
AC   B9JK76;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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   OrderedLocusNames=Arad_9233 {ECO:0000312|EMBL:ACM30318.1};
OS   Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=311403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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. {ECO:0000305|PubMed:29867142}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene does not affect growth on
CC       D-ribose and D-ribulose as a carbon source but decreases growth with D-
CC       apiose. {ECO:0000269|PubMed:29867142}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000629; ACM30318.1; -; Genomic_DNA.
DR   RefSeq; WP_015917646.1; NC_011983.1.
DR   AlphaFoldDB; B9JK76; -.
DR   SMR; B9JK76; -.
DR   STRING; 311403.Arad_9233; -.
DR   EnsemblBacteria; ACM30318; ACM30318; Arad_9233.
DR   KEGG; ara:Arad_9233; -.
DR   eggNOG; COG1879; Bacteria.
DR   HOGENOM; CLU_037628_3_2_5; -.
DR   OMA; YPEMKMV; -.
DR   OrthoDB; 1378040at2; -.
DR   Proteomes; UP000001600; Chromosome 2.
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   3: Inferred from homology;
KW   Periplasm; Reference proteome; Signal; Sugar transport; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..313
FT                   /note="D-apiose import binding protein"
FT                   /id="PRO_5002887159"
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   313 AA;  33086 MW;  D8E6B4BB440A0CB7 CRC64;
     MKLTRRLTLA AFASVLALGT AAPAFSADLI AIITPAHDNP FFKAEAVGAE AKAKELGYDT
     LVMSHDDDAN KQSEVIDTAI GRGAKAIILD NAGADATVAA IKKAKDAGIP SFLIDREINV
     TGIAVAQIVS NNYQGAQLGA QEFVKLMGEK GNYAELVGRE ADTNAGIRSQ GYHDVIDDYP
     DLKLVAKQSA NWSQTEAYAK METILQANPD IKGVISGNDT MAMGAIAALQ AAGRKDVIVV
     GFDGSNDVRD SIKAGGIKAT VMQPAYAQAQ IAVQQADAYI KNKTVPKDEK QLMDCVLINA
     DNADKLETFA LKN