TLBP_THET8
ID TLBP_THET8 Reviewed; 361 AA.
AC Q5SK82;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lactate-binding periplasmic protein TTHA0766 {ECO:0000303|PubMed:19631222};
DE AltName: Full=ABC transporter, solute-binding protein {ECO:0000312|EMBL:BAD70589.1};
DE AltName: Full=Extracytoplasmic solute receptor protein TTHA0766 {ECO:0000250|UniProtKB:P37676};
DE AltName: Full=TRAP transporter lactate-binding subunit P {ECO:0000250|UniProtKB:Q3J1R2};
DE Flags: Precursor;
GN OrderedLocusNames=TTHA0766;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1] {ECO:0000312|EMBL:BAD70589.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|PDB:2ZZW}
RP PROTEIN SEQUENCE OF 23-32, X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN
RP COMPLEXES WITH CALCIUM; LACTATE AND ZINC, FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000269|PubMed:19631222};
RX PubMed=19631222; DOI=10.1016/j.jmb.2009.07.043;
RA Akiyama N., Takeda K., Miki K.;
RT "Crystal structure of a periplasmic substrate-binding protein in complex
RT with calcium lactate.";
RL J. Mol. Biol. 392:559-565(2009).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system involved in the uptake of lactate. This protein
CC specifically binds L-lactate. {ECO:0000250|UniProtKB:P37676,
CC ECO:0000269|PubMed:19631222}.
CC -!- SUBUNIT: Homodimer. The complex comprises the extracytoplasmic solute
CC receptor protein TTHA0766, and the two putative transmembrane proteins
CC TTHA0767 and TTHA0768. {ECO:0000250|UniProtKB:P37676,
CC ECO:0000269|PubMed:19631222, ECO:0000303|PubMed:19631222}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P37676}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC {ECO:0000255}.
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DR EMBL; AP008226; BAD70589.1; -; Genomic_DNA.
DR RefSeq; WP_011228183.1; NC_006461.1.
DR RefSeq; YP_144032.1; NC_006461.1.
DR PDB; 2ZZV; X-ray; 1.40 A; A/B=1-361.
DR PDB; 2ZZW; X-ray; 1.95 A; A/B=1-361.
DR PDB; 2ZZX; X-ray; 1.75 A; A/B/C/D=1-361.
DR PDBsum; 2ZZV; -.
DR PDBsum; 2ZZW; -.
DR PDBsum; 2ZZX; -.
DR AlphaFoldDB; Q5SK82; -.
DR SMR; Q5SK82; -.
DR STRING; 300852.55772148; -.
DR EnsemblBacteria; BAD70589; BAD70589; BAD70589.
DR GeneID; 3168757; -.
DR KEGG; ttj:TTHA0766; -.
DR PATRIC; fig|300852.9.peg.759; -.
DR eggNOG; COG4663; Bacteria.
DR HOGENOM; CLU_036176_0_0_0; -.
DR OMA; GRIWASM; -.
DR PhylomeDB; Q5SK82; -.
DR EvolutionaryTrace; Q5SK82; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0031317; C:tripartite ATP-independent periplasmic transporter complex; IGC:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0015727; P:lactate transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd13681; PBP2_TRAP_lactate; 1.
DR Gene3D; 3.40.190.170; -; 1.
DR InterPro; IPR018389; DctP_fam.
DR InterPro; IPR026289; SBP_TakP-like.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR038404; TRAP_DctP_sf.
DR InterPro; IPR041721; TTHA0766.
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; Calcium; Direct protein sequencing; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:19631222"
FT CHAIN 23..361
FT /note="Lactate-binding periplasmic protein TTHA0766"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:19631222"
FT /id="PRO_0000423944"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 247..250
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19631222"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19631222"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:2ZZV"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2ZZV"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 266..300
FT /evidence="ECO:0007829|PDB:2ZZV"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 310..328
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 332..347
FT /evidence="ECO:0007829|PDB:2ZZV"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:2ZZV"
SQ SEQUENCE 361 AA; 40761 MW; EF5A2126BE41302F CRC64;
MKRVSRRAFL RRLGVGVAAT AAFSPLAVAQ ARRYRWRIQT AWDAGTVGYS LFQKFTERVK
ELTDGQLEVQ PFPAGAVVGT FDMFDAVKTG VLDGMNPFTL YWAGRMPVTA FLSSYALGLD
RPDQWETWFY SLGGLDIARR AFAEQGLFYV GPVQHDLNII HSKKPIRRFE DFKGVKLRVP
GGMIAEVFAA AGASTVLLPG GEVYPALERG VIDAADFVGP AVNYNLGFHQ VAKYIIMGPP
ETPAIHQPVD LMDFTINLNR WRSLPKPLQE RFIAAVHEYS WIHYAGIQKA NLEAWPKYRQ
AGVEVIRLSN EDVRKFRRLA IPIWFKWAKM DKYSREAFAS QLEYMKGIGY VTDEELKGLS
L
