ID   WTPA_PYRAB              Reviewed;         344 AA.
AC   Q9V2C4; G8ZFY5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Molybdate/tungstate-binding protein WtpA;
DE   Flags: Precursor;
GN   Name=wtpA; OrderedLocusNames=PYRAB01500; ORFNames=PAB0101;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Part of the ABC transporter complex WtpABC involved in
CC       molybdate/tungstate import. Binds tungstate and molybdate (By
CC       similarity). {ECO:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       WtpA subfamily. {ECO:0000305}.
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DR   EMBL; AJ248283; CAB49074.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69526.1; -; Genomic_DNA.
DR   PIR; C75203; C75203.
DR   RefSeq; WP_010867274.1; NC_000868.1.
DR   AlphaFoldDB; Q9V2C4; -.
DR   SMR; Q9V2C4; -.
DR   STRING; 272844.PAB0101; -.
DR   EnsemblBacteria; CAB49074; CAB49074; PAB0101.
DR   GeneID; 1495037; -.
DR   KEGG; pab:PAB0101; -.
DR   PATRIC; fig|272844.11.peg.163; -.
DR   eggNOG; arCOG00219; Archaea.
DR   HOGENOM; CLU_055936_0_0_2; -.
DR   OMA; KDAPNRE; -.
DR   OrthoDB; 43889at2157; -.
DR   PhylomeDB; Q9V2C4; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Metal-binding; Molybdenum; Signal; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           26..344
FT                   /note="Molybdate/tungstate-binding protein WtpA"
FT                   /id="PRO_0000159722"
FT   BINDING         40..41
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         40..41
FT                   /ligand="tungstate"
FT                   /ligand_id="ChEBI:CHEBI:46502"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         74
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         74
FT                   /ligand="tungstate"
FT                   /ligand_id="ChEBI:CHEBI:46502"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         159..161
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         159..161
FT                   /ligand="tungstate"
FT                   /ligand_id="ChEBI:CHEBI:46502"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         217
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         217
FT                   /ligand="tungstate"
FT                   /ligand_id="ChEBI:CHEBI:46502"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         235
FT                   /ligand="molybdate"
FT                   /ligand_id="ChEBI:CHEBI:36264"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
FT   BINDING         235
FT                   /ligand="tungstate"
FT                   /ligand_id="ChEBI:CHEBI:46502"
FT                   /evidence="ECO:0000250|UniProtKB:O30142"
SQ   SEQUENCE   344 AA;  38608 MW;  D6A3FC7E26658774 CRC64;
     MRLGLKIASL AIVFLILGCL GGGETETGQK TAKLIIFHAG SLSVPFSQLE SEFAKYAEKE
     LGIKVTFQDE ASGSVKAVRK VTDLGKKADI VAVADYTLIP QLMVPNYTDF YVLFATNEIV
     IAFTEKSKYA DEMLKNPDKW YEILAREDVS FGFSDPNQDP CGYRSVMVMK LADLYYGKPI
     FETLVEKTTN IYANGTHIYA PKEIIVKDKR VVIRPKETDL VGLVESGSLD YFFIYKSVAE
     QHNLKYITLP NEINLKDFSK ADFYKKVSIT LGSTGKTIYA KPIVYGITVL KDAPNRELAL
     EFLKFLLSEK GKEIFRENHQ DFLTPPVAFG NVPEEIKGLV EIKE