WTPC_ARCFU
ID WTPC_ARCFU Reviewed; 240 AA.
AC O30144;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Molybdate/tungstate import ATP-binding protein WtpC;
DE EC=7.3.2.6 {ECO:0000250|UniProtKB:Q8U4K3};
GN Name=wtpC; Synonyms=modC; OrderedLocusNames=AF_0092;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH PHOSPHATE; WTPA AND
RP WTPB, AND SUBUNIT.
RX PubMed=17322901; DOI=10.1038/nature05626;
RA Hollenstein K., Frei D.C., Locher K.P.;
RT "Structure of an ABC transporter in complex with its binding protein.";
RL Nature 446:213-216(2007).
CC -!- FUNCTION: Part of the ABC transporter complex WtpABC involved in
CC molybdate/tungstate import. Responsible for energy coupling to the
CC transport system (Probable). {ECO:0000305}.
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:0000250|UniProtKB:Q8U4K3};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (WtpC),
CC two transmembrane proteins (WtpB) and a solute-binding protein (WtpA).
CC {ECO:0000269|PubMed:17322901}.
CC -!- INTERACTION:
CC O30144; O30143: wtpB; NbExp=2; IntAct=EBI-15624339, EBI-15624357;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC Sulfate/tungstate importer (TC 3.A.1.6) family. {ECO:0000305}.
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DR EMBL; AE000782; AAB91137.1; -; Genomic_DNA.
DR PIR; D69261; D69261.
DR RefSeq; WP_010877606.1; NC_000917.1.
DR PDB; 2ONK; X-ray; 3.10 A; A/B/F/G=1-240.
DR PDBsum; 2ONK; -.
DR AlphaFoldDB; O30144; -.
DR SMR; O30144; -.
DR DIP; DIP-60272N; -.
DR IntAct; O30144; 2.
DR STRING; 224325.AF_0092; -.
DR TCDB; 3.A.1.6.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAB91137; AAB91137; AF_0092.
DR GeneID; 1483304; -.
DR KEGG; afu:AF_0092; -.
DR eggNOG; arCOG00180; Archaea.
DR HOGENOM; CLU_000604_1_22_2; -.
DR OMA; MVMEPKV; -.
DR OrthoDB; 88924at2157; -.
DR PhylomeDB; O30144; -.
DR BRENDA; 7.3.2.5; 414.
DR EvolutionaryTrace; O30144; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901238; F:ABC-type tungstate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 3D-structure; ATP-binding; Cell membrane; Membrane; Molybdenum;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..240
FT /note="Molybdate/tungstate import ATP-binding protein WtpC"
FT /id="PRO_0000338501"
FT DOMAIN 2..227
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2ONK"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:2ONK"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2ONK"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:2ONK"
SQ SEQUENCE 240 AA; 27027 MW; 7F81725C51B69379 CRC64;
MFLKVRAEKR LGNFRLNVDF EMGRDYCVLL GPTGAGKSVF LELIAGIVKP DRGEVRLNGA
DITPLPPERR GIGFVPQDYA LFPHLSVYRN IAYGLRNVER VERDRRVREM AEKLGIAHLL
DRKPARLSGG ERQRVALARA LVIQPRLLLL DEPLSAVDLK TKGVLMEELR FVQREFDVPI
LHVTHDLIEA AMLADEVAVM LNGRIVEKGK LKELFSAKNG EVAEFLSARN LLLKVSKILD
