ID   TUPA_CAMJE              Reviewed;         269 AA.
AC   Q0P885;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Tungstate-binding protein TupA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=tupA {ECO:0000303|PubMed:19818021};
GN   OrderedLocusNames=Cj1540 {ECO:0000312|EMBL:CAL35640.1};
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=19818021; DOI=10.1111/j.1365-2958.2009.06902.x;
RA   Smart J.P., Cliff M.J., Kelly D.J.;
RT   "A role for tungsten in the biology of Campylobacter jejuni: tungstate
RT   stimulates formate dehydrogenase activity and is transported via an ultra-
RT   high affinity ABC system distinct from the molybdate transporter.";
RL   Mol. Microbiol. 74:742-757(2009).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in ultra-high
CC       affinity tungstate uptake. Specifically binds tungstate.
CC       {ECO:0000269|PubMed:19818021}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TupC),
CC       two transmembrane proteins (TupB) and a solute-binding protein (TupA).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:19818021}.
CC   -!- DISRUPTION PHENOTYPE: Mutants contain the same concentration of
CC       molybdenum but they show a 75% reduction in tungsten concentration and
CC       a 50% reduction in formate dehydrogenase (FDH) activity.
CC       {ECO:0000269|PubMed:19818021}.
CC   -!- MISCELLANEOUS: Binds tungstate 50'000-fold more tightly than molybdate.
CC       {ECO:0000269|PubMed:19818021}.
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DR   EMBL; AL111168; CAL35640.1; -; Genomic_DNA.
DR   PIR; B81301; B81301.
DR   RefSeq; WP_002851335.1; NC_002163.1.
DR   RefSeq; YP_002344912.1; NC_002163.1.
DR   AlphaFoldDB; Q0P885; -.
DR   SMR; Q0P885; -.
DR   IntAct; Q0P885; 2.
DR   STRING; 192222.Cj1540; -.
DR   TCDB; 3.A.1.6.11; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q0P885; -.
DR   PRIDE; Q0P885; -.
DR   DNASU; 905822; -.
DR   EnsemblBacteria; CAL35640; CAL35640; Cj1540.
DR   GeneID; 905822; -.
DR   KEGG; cje:Cj1540; -.
DR   PATRIC; fig|192222.6.peg.1517; -.
DR   eggNOG; COG2998; Bacteria.
DR   HOGENOM; CLU_061511_0_0_7; -.
DR   OMA; LADRGTW; -.
DR   BRENDA; 7.3.2.6; 1087.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   InterPro; IPR024370; PBP_domain.
DR   Pfam; PF12849; PBP_like_2; 1.
PE   3: Inferred from homology;
KW   Periplasm; Reference proteome; Signal; Tungsten.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..269
FT                   /note="Tungstate-binding protein TupA"
FT                   /id="PRO_5004175394"
SQ   SEQUENCE   269 AA;  29801 MW;  75A2C7052F6245CC CRC64;
     MKKIISLALA LALSASAAEL KMATTTSTDN TGLLDALKPL YEKESGNTLK WVAVGTGAAL
     KMGEDCNADV LFVHSPKAEK EFMKKGFGVD RTPVMYNDFI IIADKSLASK FKGKNLKESL
     ELIKNEKLTF ISRGDKSGTD NKEKSLWKNL GGVPEKQSWY QQSGQGMLAS IKIAEEKKGV
     ILTDRGTYIK YEANEKGKPN LVIVNEGDDS LKNFYSVIAT NPKHCKNVNY TEASKFIKWV
     TSDKTLNFIA DFKLLNKPLF VIDAKTRKD