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Database: UniProt
Entry: A7IKQ4_XANP2
LinkDB: A7IKQ4_XANP2
Original site: A7IKQ4_XANP2 
ID   A7IKQ4_XANP2            Unreviewed;       324 AA.
AC   A7IKQ4;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=TRAP dicarboxylate transporter, DctP subunit {ECO:0000313|EMBL:ABS68597.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Xaut_3368 {ECO:0000313|EMBL:ABS68597.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS68597.1, ECO:0000313|Proteomes:UP000002417};
RN   [1] {ECO:0000313|EMBL:ABS68597.1, ECO:0000313|Proteomes:UP000002417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:4OVR}
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 26-324 IN COMPLEX WITH
RP   GALACTURONATE.
RX   PubMed=25540822; DOI=10.1021/bi501388y;
RA   Vetting M.W., Al-Obaidi N., Zhao S., San Francisco B., Kim J.,
RA   Wichelecki D.J., Bouvier J.T., Solbiati J.O., Vu H., Zhang X.,
RA   Rodionov D.A., Love J.D., Hillerich B.S., Seidel R.D., Quinn R.J.,
RA   Osterman A.L., Cronan J.E., Jacobson M.P., Gerlt J.A., Almo S.C.;
RT   "Experimental strategies for functional annotation and metabolism
RT   discovery: targeted screening of solute binding proteins and unbiased
RT   panning of metabolomes.";
RL   Biochemistry 54:909-931(2015).
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC       {ECO:0000256|ARBA:ARBA00009023}.
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DR   EMBL; CP000781; ABS68597.1; -; Genomic_DNA.
DR   PDB; 4OVR; X-ray; 1.65 A; A/B=26-324.
DR   PDBsum; 4OVR; -.
DR   AlphaFoldDB; A7IKQ4; -.
DR   SMR; A7IKQ4; -.
DR   STRING; 78245.Xaut_3368; -.
DR   KEGG; xau:Xaut_3368; -.
DR   eggNOG; COG1638; Bacteria.
DR   HOGENOM; CLU_036176_4_0_5; -.
DR   OrthoDB; 9803763at2; -.
DR   PhylomeDB; A7IKQ4; -.
DR   Proteomes; UP000002417; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071702; P:organic substance transport; IEA:UniProt.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd13671; PBP2_TRAP_SBP_like_3; 1.
DR   Gene3D; 3.40.190.170; Bacterial extracellular solute-binding protein, family 7; 1.
DR   InterPro; IPR018389; DctP_fam.
DR   InterPro; IPR004682; TRAP_DctP.
DR   InterPro; IPR038404; TRAP_DctP_sf.
DR   NCBIfam; TIGR00787; dctP; 1.
DR   NCBIfam; NF037995; TRAP_S1; 1.
DR   PANTHER; PTHR33376; -; 1.
DR   PANTHER; PTHR33376:SF2; 2,3-DIKETO-L-GULONATE-BINDING PERIPLASMIC PROTEIN YIAO; 1.
DR   Pfam; PF03480; DctP; 1.
DR   PIRSF; PIRSF006470; DctB; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4OVR};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002417};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..324
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002708740"
FT   BINDING         34
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
FT   BINDING         72
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
FT   BINDING         88
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
FT   BINDING         148
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
FT   BINDING         168
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
FT   BINDING         208
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
FT   BINDING         209
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
FT   BINDING         235
FT                   /ligand="beta-D-galacturonate"
FT                   /ligand_id="ChEBI:CHEBI:85312"
FT                   /evidence="ECO:0007829|PDB:4OVR"
SQ   SEQUENCE   324 AA;  35649 MW;  7AD42E7589540DC3 CRC64;
     MKGLALYVAA AMTSVIALTP LAAQARQYRS ADVQPADYPT VKAVQSMSDE LNKETNGKIS
     IKVFPNSQLG SEKDTIEQVK LGALDFIRIN SGTLNTVCPA MTVPVLPFLF RDKAHMRAVL
     DGPIGDEILA DCASHGLVGL AFYDSGARSF YATTPIRKLE DLKGKKIRVQ QSDIWVSMMK
     LLGANATPMP AGEVFTGLKS GLIDGAENNW PSYDNFHHYE AAKNYSLSEH SMAPEVLLIS
     KRVFDSFTPE EQVQVRKAAK NSVGYMRQLW DAMEISSREK VEKAGVEVIT IDKAPFQAAV
     QPLYDQFVTD PKLKDMITRI KAAQ
//
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