APIBP_RHIEC
ID APIBP_RHIEC Reviewed; 313 AA.
AC Q2JZQ5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=RHE_PF00037 {ECO:0000312|EMBL:ABC93931.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid p42f.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN [2] {ECO:0007744|PDB:4RY0, ECO:0007744|PDB:5IBQ}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 27-313 IN COMPLEXES WITH D-RIBOSE
RP AND D-APIOSE, AND FUNCTION.
RC STRAIN=CFN 42 / ATCC 51251;
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; CP000138; ABC93931.1; -; Genomic_DNA.
DR RefSeq; WP_011428349.1; NC_007766.1.
DR PDB; 4RY0; X-ray; 1.40 A; A=27-313.
DR PDB; 5IBQ; X-ray; 1.20 A; A=27-313.
DR PDBsum; 4RY0; -.
DR PDBsum; 5IBQ; -.
DR AlphaFoldDB; Q2JZQ5; -.
DR SMR; Q2JZQ5; -.
DR EnsemblBacteria; ABC93931; ABC93931; RHE_PF00037.
DR KEGG; ret:RHE_PF00037; -.
DR HOGENOM; CLU_037628_3_2_5; -.
DR OMA; YPEMKMV; -.
DR Proteomes; UP000001936; Plasmid p42f.
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 3D-structure; Periplasm; Plasmid; Reference proteome; Signal;
KW 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_5004211155"
FT BINDING 39
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000305|PubMed:29867142"
FT BINDING 115..116
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000305|PubMed:29867142"
FT BINDING 162..164
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000305|PubMed:29867142"
FT BINDING 168
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000305|PubMed:29867142"
FT BINDING 218
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000305|PubMed:29867142"
FT BINDING 243
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000305|PubMed:29867142"
FT BINDING 263
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000305|PubMed:29867142"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5IBQ"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:5IBQ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 265..282
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:5IBQ"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:5IBQ"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:5IBQ"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:5IBQ"
SQ SEQUENCE 313 AA; 33059 MW; 6BD494BA131B09EB CRC64;
MKLTRRLTLA AFASALALGT AMPAFAADLI AIITPAHDNP FFKAEAVGAE AKAKELGYET
LVMTHDDDAN KQSEMIDTAI GRGAKAIILD NAGADASVAA VKKAKDAGIP SFLIDREINA
TGVAVAQIVS NNYQGAQLGA QEFVKLMGEK GNYVELVGKE SDTNAGIRSQ GYHDVIDDYP
EMKSVAKQSA NWSQTEAYSK METILQANPD IKGVISGNDT MAMGAIAALQ AAGRKDVIVV
GFDGSNDVRD SIKSGGIKAT VLQPAYAQAQ LAVEQADAYI KNKTTPKEEK QLMDCVLINA
DNAGKLETFA LTN
