WTPB_ARCFU
ID WTPB_ARCFU Reviewed; 261 AA.
AC O30143;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Molybdate/tungstate transport system permease protein WtpB;
GN Name=wtpB; Synonyms=modB; OrderedLocusNames=AF_0093;
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 WTPA AND WTPC,
RP TOPOLOGY, 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. Probably responsible for the translocation
CC of the substrate across the membrane (Probable). {ECO:0000305}.
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 O30143; O30144: wtpC; NbExp=2; IntAct=EBI-15624357, EBI-15624339;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; AE000782; AAB91136.1; -; Genomic_DNA.
DR PIR; E69261; E69261.
DR RefSeq; WP_010877607.1; NC_000917.1.
DR PDB; 2ONK; X-ray; 3.10 A; C/D/H/I=1-261.
DR PDBsum; 2ONK; -.
DR AlphaFoldDB; O30143; -.
DR SMR; O30143; -.
DR DIP; DIP-60273N; -.
DR IntAct; O30143; 2.
DR STRING; 224325.AF_0093; -.
DR TCDB; 3.A.1.6.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAB91136; AAB91136; AF_0093.
DR GeneID; 24793648; -.
DR KEGG; afu:AF_0093; -.
DR eggNOG; arCOG00164; Archaea.
DR HOGENOM; CLU_016047_14_1_2; -.
DR OMA; NEYNFVA; -.
DR OrthoDB; 97465at2157; -.
DR PhylomeDB; O30143; -.
DR EvolutionaryTrace; O30143; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Molybdenum; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..261
FT /note="Molybdate/tungstate transport system permease
FT protein WtpB"
FT /id="PRO_0000338496"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17322901"
FT TRANSMEM 3..28
FT /note="Helical; Name=1"
FT TOPO_DOM 29..46
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:17322901"
FT TRANSMEM 47..76
FT /note="Helical; Name=2"
FT TOPO_DOM 77..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17322901"
FT TRANSMEM 86..110
FT /note="Helical; Name=3"
FT TOPO_DOM 111..123
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:17322901"
FT TRANSMEM 124..154
FT /note="Helical; Name=4"
FT TOPO_DOM 155..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17322901"
FT TRANSMEM 185..209
FT /note="Helical; Name=5"
FT TOPO_DOM 210..230
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:17322901"
FT TRANSMEM 231..251
FT /note="Helical; Name=6"
FT TOPO_DOM 252..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17322901"
FT DOMAIN 51..247
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 93..107
FT /note="Gate 1"
FT REGION 193..203
FT /note="Gate 2"
FT HELIX 2..29
FT /evidence="ECO:0007829|PDB:2ONK"
FT TURN 30..34
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 45..77
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:2ONK"
FT TURN 115..119
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 128..153
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 177..198
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2ONK"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:2ONK"
SQ SEQUENCE 261 AA; 27833 MW; C11342F58293B77F CRC64;
MRLLFSALLA LLSSIILLFV LLPVAATVTL QLFNFDEFLK AASDPAVWKV VLTTYYAALI
STLIAVIFGT PLAYILARKS FPGKSVVEGI VDLPVVIPHT VAGIALLVVF GSSGLIGSFS
PLKFVDALPG IVVAMLFVSV PIYINQAKEG FASVDVRLEH VARTLGSSPL RVFFTVSLPL
SVRHIVAGAI MSWARGISEF GAVVVIAYYP MIAPTLIYER YLSEGLSAAM PVAAILILLS
LAVFVALRII VGREDVSEGQ G
