TAKP_CERS4
ID TAKP_CERS4 Reviewed; 365 AA.
AC Q3J1R2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Alpha-keto acid-binding periplasmic protein TakP {ECO:0000250|UniProtKB:P44542, ECO:0000303|PubMed:17362499};
DE AltName: Full=Extracytoplasmic solute receptor protein TakP {ECO:0000303|PubMed:17362499};
DE AltName: Full=TRAP transporter alpha-keto acid-binding subunit P {ECO:0000303|PubMed:17362499};
DE AltName: Full=TRAP-T family sorbitol/mannitol transporter, periplasmic binding protein, SmoM {ECO:0000312|EMBL:ABA79272.1};
DE Flags: Precursor;
GN Name=takP {ECO:0000303|PubMed:17362499};
GN Synonyms=smoM {ECO:0000312|EMBL:ABA79272.1}; OrderedLocusNames=RHOS4_17040;
GN ORFNames=RSP_0097;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1] {ECO:0000312|EMBL:ABA79272.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|PDB:2HZK}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF UNLIGANDED FORM AND IN COMPLEX
RP WITH PYRUVATE AND SODIUM, FUNCTION, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000269|PubMed:17362499};
RX PubMed=17362499; DOI=10.1186/1472-6807-7-11;
RA Gonin S., Arnoux P., Pierru B., Lavergne J., Alonso B., Sabaty M.,
RA Pignol D.;
RT "Crystal structures of an extracytoplasmic solute receptor from a TRAP
RT transporter in its open and closed forms reveal a helix-swapped dimer
RT requiring a cation for alpha-keto acid binding.";
RL BMC Struct. Biol. 7:11-11(2007).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system TakPQM involved in the uptake of alpha-keto acids.
CC This protein specifically binds alpha-keto acids including pyruvate,
CC oxobutyrate, oxovalerate and 4-methyl-2-oxovalerate. Ligand-binding
CC affinity increases with the increasing chain length of the aliphatic
CC backbone of the ligand. Is not able to bind alpha-ketoglutarate.
CC {ECO:0000250|UniProtKB:P44542, ECO:0000269|PubMed:17362499}.
CC -!- SUBUNIT: Homodimer. The complex comprises the extracytoplasmic solute
CC receptor protein TakP, and the two transmembrane proteins TakQ and
CC TakM. {ECO:0000250|UniProtKB:P44542, ECO:0000269|PubMed:17362499,
CC ECO:0000303|PubMed:17362499}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P44542}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC {ECO:0000255}.
CC -!- CAUTION: Was originally (Ref.1) annotated as coding for a
CC sorbitol/mannitol-binding protein based solely on its position in the
CC genome close to the smo operon encoding known sorbitol/mannitol
CC catabolic genes. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000143; ABA79272.1; -; Genomic_DNA.
DR RefSeq; WP_011337992.1; NZ_CP030271.1.
DR RefSeq; YP_353173.1; NC_007493.2.
DR PDB; 2HZK; X-ray; 1.70 A; A/B/C/D=1-365.
DR PDB; 2HZL; X-ray; 1.40 A; A/B=1-365.
DR PDBsum; 2HZK; -.
DR PDBsum; 2HZL; -.
DR AlphaFoldDB; Q3J1R2; -.
DR SMR; Q3J1R2; -.
DR STRING; 272943.RSP_0097; -.
DR EnsemblBacteria; ABA79272; ABA79272; RSP_0097.
DR KEGG; rsp:RSP_0097; -.
DR PATRIC; fig|272943.9.peg.2037; -.
DR eggNOG; COG4663; Bacteria.
DR OMA; FWEGGPT; -.
DR PhylomeDB; Q3J1R2; -.
DR EvolutionaryTrace; Q3J1R2; -.
DR PRO; PR:Q3J1R2; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0031317; C:tripartite ATP-independent periplasmic transporter complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0043177; F:organic acid binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0015849; P:organic acid transport; IEA:InterPro.
DR GO; GO:0071702; P:organic substance transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd13682; PBP2_TRAP_alpha-ketoacid; 1.
DR Gene3D; 3.40.190.170; -; 1.
DR InterPro; IPR018389; DctP_fam.
DR InterPro; IPR026289; SBP_TakP-like.
DR InterPro; IPR041722; TakP/all3028.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR038404; TRAP_DctP_sf.
DR PANTHER; PTHR33376; PTHR33376; 1.
DR Pfam; PF03480; DctP; 1.
DR PIRSF; PIRSF039026; SiaP; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Periplasm; Pyruvate; Reference proteome;
KW Signal; Sodium; Transport.
FT SIGNAL 1..26
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 27..365
FT /note="Alpha-keto acid-binding periplasmic protein TakP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423664"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17362499"
FT BINDING 156
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:17362499"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17362499"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17362499"
FT BINDING 214
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:17362499"
FT BINDING 215
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:17362499"
FT BINDING 240
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:17362499"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:2HZL"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:2HZL"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:2HZL"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2HZL"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2HZL"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:2HZL"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2HZK"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 259..293
FT /evidence="ECO:0007829|PDB:2HZL"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 303..323
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 325..344
FT /evidence="ECO:0007829|PDB:2HZL"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:2HZL"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:2HZL"
SQ SEQUENCE 365 AA; 39984 MW; 6070412E72576B26 CRC64;
MDRRSFITKA AVGGAAASAL AAPALAQSAP KVTWRLASSF PKSLDTIFGG AEVLSKMLSE
ATDGNFQIQV FSAGELVPGL QAADAVTEGT VECCHTVGYY YWGKDPTFAL AAAVPFSLSA
RGINAWHYHG GGIDLYNEFL SQHNIVAFPG GNTGVQMGGW FRREINTVAD MQGLKMRVGG
FAGKVMERLG VVPQQIAGGD IYPALEKGTI DATEWVGPYD DEKLGFFKVA PYYYYPGWWE
GGPTVHFMFN KSAYEGLTPT YQSLLRTACH AADANMLQLY DWKNPTAIKS LVAQGTQLRP
FSPEILQACF EAANEVYAEM EASNPAFKKI WDSIKAFRSE HYTWAQIAEY NYDTFMMVQQ
NAGKL
