APIBP_ACTSZ
ID APIBP_ACTSZ Reviewed; 310 AA.
AC A6VKQ8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=Asuc_0175 {ECO:0000312|EMBL:ABR73555.1};
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
RN [2]
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; CP000746; ABR73555.1; -; Genomic_DNA.
DR RefSeq; WP_011978831.1; NC_009655.1.
DR AlphaFoldDB; A6VKQ8; -.
DR SMR; A6VKQ8; -.
DR STRING; 339671.Asuc_0175; -.
DR EnsemblBacteria; ABR73555; ABR73555; Asuc_0175.
DR KEGG; asu:Asuc_0175; -.
DR eggNOG; COG1879; Bacteria.
DR HOGENOM; CLU_037628_3_2_6; -.
DR OMA; YPEMKMV; -.
DR OrthoDB; 1378040at2; -.
DR Proteomes; UP000001114; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
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; Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..310
FT /note="D-apiose import binding protein"
FT /id="PRO_5002701886"
FT BINDING 35
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 111..112
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 158..160
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 164
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 214
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 239
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
FT BINDING 260
FT /ligand="D-apiofuranose"
FT /ligand_id="ChEBI:CHEBI:141215"
FT /evidence="ECO:0000250|UniProtKB:Q2JZQ5"
SQ SEQUENCE 310 AA; 33123 MW; 3E02C228F3327073 CRC64;
MKLLKASLVA LSLAASTFVY ADNGLIAIIT PSHDNPFFKA EADGAKQKAE ELGYTTLVAS
HDDDANKQDQ LISTAVSRKA KAIILDNAGS DVTVGALEKA KAAGVPAFLI DREINKTGVA
VSQIVSNNYQ GAQLSAEKFV ELMGEKGQYV ELLGRESDTN ASVRSQGFHE IIDEYPEMKM
VAQQTANWSQ TEGFSRMESI LQANPNIKGV ISGNDTMALG AEAALKAAGR TDVIVVGFDG
SDYVRDSILA GGNIKATALQ PAWDQAQEAV VQADKYIRTG STGKEEKQLM DCILIDSSNA
KKLNKFSLSK