TMBP_NOSS1
ID TMBP_NOSS1 Reviewed; 364 AA.
AC Q8YSQ6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Monocarboxylate 2-oxoacid-binding periplasmic protein all3028 {ECO:0000250|UniProtKB:Q3J1R2, ECO:0000303|PubMed:20851902};
DE AltName: Full=Extracellular solute-binding protein {ECO:0000312|EMBL:BAB74727.1};
DE AltName: Full=Extracytoplasmic solute receptor protein all3028 {ECO:0000250|UniProtKB:Q3J1R2};
DE AltName: Full=TRAP transporter monocarboxylate 2-oxoacid-binding subunit P {ECO:0000250|UniProtKB:Q3J1R2, ECO:0000303|PubMed:20851902};
DE Flags: Precursor;
GN OrderedLocusNames=all3028;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1] {ECO:0000312|EMBL:BAB74727.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576 {ECO:0000269|PubMed:20851902};
RX PubMed=20851902; DOI=10.1128/jb.00982-10;
RA Pernil R., Herrero A., Flores E.;
RT "A TRAP transporter for pyruvate and other monocarboxylate 2-oxoacids in
RT the cyanobacterium Anabaena sp. strain PCC 7120.";
RL J. Bacteriol. 192:6089-6092(2010).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system involved in the uptake of monocarboxylate 2-oxoacids.
CC This protein specifically binds monocarboxylate 2-oxoacids including
CC pyruvate, 2-oxobutyrate, 2-oxovalerate, 2-oxoisovalerate, 2-
CC oxoisocaproate and 2-oxo-3-methylvalerate. Is not able to bind
CC mannitol. {ECO:0000269|PubMed:20851902}.
CC -!- ACTIVITY REGULATION: Pyruvate uptake inhibited by 2-oxobutyrate, 2-
CC oxovalerate, 2-oxoisovalerate, 2-oxoisocaproate and 2-oxo-3-
CC methylvalerate. {ECO:0000269|PubMed:20851902}.
CC -!- SUBUNIT: Homodimer. The complex comprises the extracytoplasmic solute
CC receptor protein all3028, and the two putative transmembrane proteins
CC alr3026 and alr3027 (By similarity). {ECO:0000250|UniProtKB:Q3J1R2,
CC ECO:0000269|PubMed:20851902}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P44542}.
CC -!- DISRUPTION PHENOTYPE: Impaired pyruvate uptake.
CC {ECO:0000269|PubMed:20851902}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC {ECO:0000255}.
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DR EMBL; BA000019; BAB74727.1; -; Genomic_DNA.
DR PIR; AE2184; AE2184.
DR RefSeq; WP_010997179.1; NZ_RSCN01000050.1.
DR AlphaFoldDB; Q8YSQ6; -.
DR SMR; Q8YSQ6; -.
DR STRING; 103690.17132122; -.
DR TCDB; 2.A.56.3.3; the tripartite atp-independent periplasmic transporter (trap-t) family.
DR EnsemblBacteria; BAB74727; BAB74727; BAB74727.
DR KEGG; ana:all3028; -.
DR eggNOG; COG4663; Bacteria.
DR OMA; FWEGGPT; -.
DR OrthoDB; 1251304at2; -.
DR Proteomes; UP000002483; 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:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0043177; F:organic acid binding; ISS:UniProtKB.
DR GO; GO:0005342; F:organic acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015849; P:organic acid transport; IMP:UniProtKB.
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; IPR038404; TRAP_DctP_sf.
DR PANTHER; PTHR33376; PTHR33376; 1.
DR Pfam; PF03480; DctP; 1.
DR PIRSF; PIRSF039026; SiaP; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Periplasm; Reference proteome; Signal; Sodium; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT CHAIN 27..364
FT /note="Monocarboxylate 2-oxoacid-binding periplasmic
FT protein all3028"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT /id="PRO_0000423665"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT BINDING 160
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT BINDING 218
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT BINDING 219
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
FT BINDING 244
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q3J1R2"
SQ SEQUENCE 364 AA; 40012 MW; 5E54C4C3D18207A9 CRC64;
MKRREVLNTA AIATATTALV SCTQTNTSSV QAGLPNVRWR MTTSWPKSLG TFIGAETVAK
RVAEMTNGRF KITPFAAGEL VPGLQVLDAV QAGTVECGHT SSYYYIGKSP ALAFATSVPF
GLNAQQQYAW LYQGGGLAAI QKIYANFNVI NFPAGSTGAQ MGGWFKKEIK SVSDLKGLKM
RIPGLGGQVM SRLGVNVQVL PGGEIYLALD RGAIDAAEWV GPYDDEKLGL NKAAQFYYYP
GWWEPGPTLD VLVNLNAWNR LPKEYQEIFK TATVEANLTM LNQYDALNGE ALTRLLAGGT
KLVPYSQEIM QAAQKISFDI FEENASKDAA FKQVYEQWKA FRKQIFAWNR VNELSYENFA
SSSQ
