WTPA_ARCFU
ID WTPA_ARCFU Reviewed; 342 AA.
AC O30142;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Molybdate/tungstate-binding protein WtpA;
DE Flags: Precursor;
GN Name=wtpA; Synonyms=modA; OrderedLocusNames=AF_0094;
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] {ECO:0007744|PDB:2ONK, ECO:0007744|PDB:2ONR, ECO:0007744|PDB:2ONS}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 32-342 IN COMPLEXES WITH
RP MOLYBDATE; TUNGSTATE; WTPB AND WTPC, 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. Binds tungstate and molybdate.
CC {ECO:0000269|PubMed:17322901}.
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 -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC WtpA subfamily. {ECO:0000305}.
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DR EMBL; AE000782; AAB91135.1; -; Genomic_DNA.
DR PIR; F69261; F69261.
DR RefSeq; WP_010877608.1; NC_000917.1.
DR PDB; 2ONK; X-ray; 3.10 A; E/J=32-342.
DR PDB; 2ONR; X-ray; 1.60 A; A=32-342.
DR PDB; 2ONS; X-ray; 1.55 A; A=32-342.
DR PDB; 3CIJ; X-ray; 1.07 A; A/B=32-323.
DR PDBsum; 2ONK; -.
DR PDBsum; 2ONR; -.
DR PDBsum; 2ONS; -.
DR PDBsum; 3CIJ; -.
DR AlphaFoldDB; O30142; -.
DR SMR; O30142; -.
DR DIP; DIP-60274N; -.
DR IntAct; O30142; 2.
DR STRING; 224325.AF_0094; -.
DR TCDB; 3.A.1.6.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAB91135; AAB91135; AF_0094.
DR GeneID; 1483306; -.
DR KEGG; afu:AF_0094; -.
DR eggNOG; arCOG00219; Archaea.
DR HOGENOM; CLU_055936_0_0_2; -.
DR OMA; GYRTVMM; -.
DR OrthoDB; 43889at2157; -.
DR PhylomeDB; O30142; -.
DR EvolutionaryTrace; O30142; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901359; F:tungstate binding; IEA:InterPro.
DR InterPro; IPR022498; ABC_trnspt_W-bd_WtpA.
DR TIGRFAMs; TIGR03730; tungstate_WtpA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Metal-binding; Molybdenum;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..342
FT /note="Molybdate/tungstate-binding protein WtpA"
FT /id="PRO_0000159717"
FT BINDING 41..42
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONR"
FT BINDING 41..42
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONK"
FT BINDING 70
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONR"
FT BINDING 70
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONK"
FT BINDING 153..155
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONR"
FT BINDING 153..155
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONK"
FT BINDING 218
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONR"
FT BINDING 218
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONK"
FT BINDING 236
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONR"
FT BINDING 236
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:17322901,
FT ECO:0007744|PDB:2ONK"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:3CIJ"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3CIJ"
FT TURN 124..128
FT /evidence="ECO:0007829|PDB:3CIJ"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3CIJ"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 154..169
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3CIJ"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3CIJ"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:3CIJ"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2ONK"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:3CIJ"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:3CIJ"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:2ONS"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2ONS"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2ONS"
SQ SEQUENCE 342 AA; 38630 MW; 2DACAF169A074406 CRC64;
MHIGGGVVKI RILILLMLAL FLLGCSSNVN TNVKLKVFHA GSLTEPMKAF KRAFEEKHPN
VEVQTEAAGS AATIRKVTEL GRKADVIATA DYTLIQKMMY PEFANWTIMF AKNQIVLAYR
NDSRYADEIN SQNWYEILKR PDVRFGFSNP NDDPCGYRSL MAIQLAELYY NDPTIFDELV
AKNSNLRFSE DNGSYVLRMP SSERIEINKS KIMIRSMEME LIHLVESGEL DYFFIYKSVA
KQHGFNFVEL PVEIDLSSPD YAELYSKVKV VLANGKEVTG KPIVYGITIP KNAENRELAV
EFVKLVISEE GQEILRELGQ EPLVPPRADT AVPSLKAMVE VS
