ID   TUPC_CAMJE              Reviewed;         331 AA.
AC   Q0P887;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Tungstate uptake system ATP-binding protein TupC {ECO:0000305};
DE            EC=7.3.2.6 {ECO:0000305|PubMed:19818021};
GN   Name=tupC {ECO:0000303|PubMed:19818021};
GN   OrderedLocusNames=Cj1538c {ECO:0000312|EMBL:CAL35638.1};
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   PROBABLE FUNCTION IN TUNGSTATE UPTAKE.
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. Probably responsible for energy coupling to
CC       the transport system. {ECO:0000305|PubMed:19818021}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + tungstate(in) = ADP + H(+) + phosphate +
CC         tungstate(out); Xref=Rhea:RHEA:35027, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46502, ChEBI:CHEBI:456216; EC=7.3.2.6;
CC         Evidence={ECO:0000305|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   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AL111168; CAL35638.1; -; Genomic_DNA.
DR   PIR; H81300; H81300.
DR   RefSeq; WP_002868367.1; NC_002163.1.
DR   RefSeq; YP_002344910.1; NC_002163.1.
DR   AlphaFoldDB; Q0P887; -.
DR   SMR; Q0P887; -.
DR   IntAct; Q0P887; 5.
DR   STRING; 192222.Cj1538c; -.
DR   TCDB; 3.A.1.6.11; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q0P887; -.
DR   PRIDE; Q0P887; -.
DR   EnsemblBacteria; CAL35638; CAL35638; Cj1538c.
DR   GeneID; 905820; -.
DR   KEGG; cje:Cj1538c; -.
DR   PATRIC; fig|192222.6.peg.1515; -.
DR   eggNOG; COG3839; Bacteria.
DR   HOGENOM; CLU_000604_1_1_7; -.
DR   OMA; FGPMNLK; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:1901238; F:ABC-type tungstate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..331
FT                   /note="Tungstate uptake system ATP-binding protein TupC"
FT                   /id="PRO_0000435511"
FT   DOMAIN          2..230
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   331 AA;  38834 MW;  92D378C4CEA750BD CRC64;
     MIEISNLFFN YQNKEVLKIK NLKLDTSKIS ILMGANGSGK STFLRILKFL EGDFSKNISY
     FGNFKPNNKQ KREIYLLFPE PILLNRSVRA NFLFTLKTYG IKEDIEERIK ESLMFLNLDE
     SLLSKHPNEL SSGQSQKIAF AIALSVRAKY YLLDEPSAFL DKNTTLLFKK TILKMHENFN
     TGFLIASHDK HFLDSLAQKK LYLHSGEILE FENTNVFELE NQGVKFCNFI DFSNCKKYKD
     FKKPPSKIAI DPYKISFFNS KNIPKNNYDF ILEKCYIIAL RSRKSDVFIR VSCMDKILEF
     ALEKQEFLRF DLKLYEELSL YFYEDAICFL N