WTPA_PYRFU
ID WTPA_PYRFU Reviewed; 345 AA.
AC Q8U4K5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Molybdate/tungstate-binding protein WtpA {ECO:0000305};
DE Flags: Precursor;
GN Name=wtpA {ECO:0000303|PubMed:16952940}; OrderedLocusNames=PF0080;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, GENE NAME, AND SUBUNIT.
RX PubMed=16952940; DOI=10.1128/jb.00548-06;
RA Bevers L.E., Hagedoorn P.-L., Krijger G.C., Hagen W.R.;
RT "Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first
RT member of a new class of tungstate and molybdate transporters.";
RL J. Bacteriol. 188:6498-6505(2006).
RN [3] {ECO:0007744|PDB:3CG1}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 32-324 IN COMPLEX WITH TUNGSTATE.
RX PubMed=19234723; DOI=10.1007/s00775-009-0479-7;
RA Hollenstein K., Comellas-Bigler M., Bevers L.E., Feiters M.C.,
RA Meyer-Klaucke W., Hagedoorn P.L., Locher K.P.;
RT "Distorted octahedral coordination of tungstate in a subfamily of specific
RT binding proteins.";
RL J. Biol. Inorg. Chem. 14:663-672(2009).
CC -!- FUNCTION: Part of the ABC transporter complex WtpABC involved in
CC molybdate/tungstate import. Binds tungstate and molybdate, with a
CC preference for tungstate. {ECO:0000269|PubMed:16952940}.
CC -!- SUBUNIT: Monomer (PubMed:16952940). The complex is composed of two ATP-
CC binding proteins (WtpC), two transmembrane proteins (WtpB) and a
CC solute-binding protein (WtpA) (Probable). {ECO:0000269|PubMed:16952940,
CC ECO:0000305}.
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; AE009950; AAL80204.1; -; Genomic_DNA.
DR PDB; 3CG1; X-ray; 1.60 A; A/B=32-324.
DR PDBsum; 3CG1; -.
DR AlphaFoldDB; Q8U4K5; -.
DR SMR; Q8U4K5; -.
DR STRING; 186497.PF0080; -.
DR TCDB; 3.A.1.6.5; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAL80204; AAL80204; PF0080.
DR KEGG; pfu:PF0080; -.
DR PATRIC; fig|186497.12.peg.84; -.
DR eggNOG; arCOG00219; Archaea.
DR HOGENOM; CLU_055936_0_0_2; -.
DR OMA; KDAPNRE; -.
DR PhylomeDB; Q8U4K5; -.
DR BRENDA; 7.3.2.6; 5243.
DR EvolutionaryTrace; Q8U4K5; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Metal-binding; Molybdenum;
KW Reference proteome; Signal; Transport; Tungsten.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..345
FT /note="Molybdate/tungstate-binding protein WtpA"
FT /id="PRO_0000159723"
FT BINDING 41..42
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:O30142"
FT BINDING 41..42
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:19234723,
FT ECO:0007744|PDB:3CG1"
FT BINDING 75
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:O30142"
FT BINDING 75
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:19234723,
FT ECO:0007744|PDB:3CG1"
FT BINDING 160..162
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:O30142"
FT BINDING 160..162
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:19234723,
FT ECO:0007744|PDB:3CG1"
FT BINDING 218
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:O30142"
FT BINDING 218
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:19234723,
FT ECO:0007744|PDB:3CG1"
FT BINDING 236
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:O30142"
FT BINDING 236
FT /ligand="tungstate"
FT /ligand_id="ChEBI:CHEBI:46502"
FT /evidence="ECO:0000269|PubMed:19234723,
FT ECO:0007744|PDB:3CG1"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 44..62
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:3CG1"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3CG1"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 161..177
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:3CG1"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3CG1"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3CG1"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3CG1"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3CG1"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:3CG1"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:3CG1"
SQ SEQUENCE 345 AA; 38801 MW; FC52F08CFA995DD7 CRC64;
MREGGVMKKR LLALIVAFAV LTAGCLGSES KEVTLIVFHA GSLSVPFQEV EKEFSEYAER
NLGIKVSFQD EASGSVMAVR KVTDLGRKAD VIGVADYTLI PQLLIPNYTD FYVLFATNEI
VIAFTDKSRY VEEMKSNPDK WYEILAREDV RFGFSDPNQD PCGYRSLMVI KLADLYYGKE
IFKELIEENT NIYSNGTQIY APKEITVNPG KIVIRPKETD LLGLVESGSI DYIFIYKSVA
KQHNLSYITL PSEINLGDFS KEKFYGQISI TLGSTGKTIK AKPIVYGVTV LKDAPNREVA
IEFLRYLLSE NGKRIFEKNH QDFLEPPIAF GNVPEELKPL VSIEK
