GLCV_SACS2
ID GLCV_SACS2 Reviewed; 353 AA.
AC Q97UY8;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glucose import ATP-binding protein GlcV {ECO:0000305};
DE EC=7.5.2.- {ECO:0000305|PubMed:10400586};
GN Name=glcV {ECO:0000303|PubMed:11260467};
GN OrderedLocusNames=SSO2850 {ECO:0000312|EMBL:AAK42960.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10400586; DOI=10.1128/jb.181.14.4285-4291.1999;
RA Albers S.V., Elferink M.G., Charlebois R.L., Sensen C.W., Driessen A.J.,
RA Konings W.N.;
RT "Glucose transport in the extremely thermoacidophilic Sulfolobus
RT solfataricus involves a high-affinity membrane-integrated binding
RT protein.";
RL J. Bacteriol. 181:4285-4291(1999).
RN [3]
RP NOMENCLATURE, AND FUNCTION.
RX PubMed=11260467; DOI=10.1046/j.1365-2958.2001.02336.x;
RA Elferink M.G., Albers S.V., Konings W.N., Driessen A.J.;
RT "Sugar transport in Sulfolobus solfataricus is mediated by two families of
RT binding protein-dependent ABC transporters.";
RL Mol. Microbiol. 39:1494-1503(2001).
RN [4]
RP ATPASE ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND CRYSTALLIZATION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11807278; DOI=10.1107/s0907444901020765;
RA Verdon G., Albers S.V., Dijkstra B.W., Driessen A.J., Thunnissen A.M.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of an archaeal ABC-ATPase.";
RL Acta Crystallogr. D 58:362-365(2002).
RN [5] {ECO:0007744|PDB:1OXS, ECO:0007744|PDB:1OXT, ECO:0007744|PDB:1OXU, ECO:0007744|PDB:1OXV}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH
RP ADP AND ATP ANALOG, FUNCTION, AND DOMAIN.
RX PubMed=12823973; DOI=10.1016/s0022-2836(03)00575-8;
RA Verdon G., Albers S.V., Dijkstra B.W., Driessen A.J., Thunnissen A.M.;
RT "Crystal structures of the ATPase subunit of the glucose ABC transporter
RT from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound
RT conformations.";
RL J. Mol. Biol. 330:343-358(2003).
RN [6] {ECO:0007744|PDB:1OXX}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF MUTANT ALA-144, FUNCTION, ATPASE
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF SER-142; GLY-144 AND GLU-166.
RX PubMed=14607117; DOI=10.1016/j.jmb.2003.08.065;
RA Verdon G., Albers S.V., van Oosterwijk N., Dijkstra B.W., Driessen A.J.,
RA Thunnissen A.M.;
RT "Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase
RT from Sulfolobus solfataricus.";
RL J. Mol. Biol. 334:255-267(2003).
CC -!- FUNCTION: Part of the ABC transporter complex GlcSTUV involved in
CC glucose uptake (Probable). Responsible for energy coupling to the
CC transport system (PubMed:12823973, PubMed:14607117). In vitro, as a
CC free subunit, exhibits a constitutive ATPase activity
CC (PubMed:11807278). {ECO:0000269|PubMed:11807278,
CC ECO:0000269|PubMed:12823973, ECO:0000269|PubMed:14607117,
CC ECO:0000305|PubMed:10400586, ECO:0000305|PubMed:11260467}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose(out) + H2O = ADP + D-glucose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:60184, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:10400586};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60185;
CC Evidence={ECO:0000305|PubMed:10400586};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=290 uM for ATP {ECO:0000269|PubMed:11807278};
CC pH dependence:
CC Optimum pH is 6.5 for ATPase activity. {ECO:0000269|PubMed:11807278};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GlcV),
CC two transmembrane proteins (GlcT and GlcU) and a solute-binding protein
CC (GlcS) (Probable). Forms transient head-to-tail homodimers in the
CC presence of ATP-Mg(2+) (PubMed:14607117). {ECO:0000269|PubMed:14607117,
CC ECO:0000305|PubMed:10400586}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: Consists of a typical ABC-ATPase domain, comprising two
CC subdomains, connected by a linker region to a C-terminal domain of
CC unknown function. {ECO:0000269|PubMed:12823973}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
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DR EMBL; AE006641; AAK42960.1; -; Genomic_DNA.
DR PIR; A90463; A90463.
DR RefSeq; WP_010924001.1; NC_002754.1.
DR PDB; 1OXS; X-ray; 1.65 A; C=1-353.
DR PDB; 1OXT; X-ray; 2.10 A; A/B/D=1-353.
DR PDB; 1OXU; X-ray; 2.10 A; A/B/C=1-353.
DR PDB; 1OXV; X-ray; 1.95 A; A/B/D=1-353.
DR PDB; 1OXX; X-ray; 1.45 A; K=1-353.
DR PDBsum; 1OXS; -.
DR PDBsum; 1OXT; -.
DR PDBsum; 1OXU; -.
DR PDBsum; 1OXV; -.
DR PDBsum; 1OXX; -.
DR AlphaFoldDB; Q97UY8; -.
DR SMR; Q97UY8; -.
DR STRING; 273057.SSO2850; -.
DR TCDB; 3.A.1.1.13; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAK42960; AAK42960; SSO2850.
DR GeneID; 27429116; -.
DR KEGG; sso:SSO2850; -.
DR PATRIC; fig|273057.12.peg.2936; -.
DR eggNOG; arCOG00175; Archaea.
DR HOGENOM; CLU_000604_1_1_2; -.
DR InParanoid; Q97UY8; -.
DR OMA; EFVGTMS; -.
DR PhylomeDB; Q97UY8; -.
DR BRENDA; 7.5.2.B8; 6163.
DR EvolutionaryTrace; Q97UY8; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR GO; GO:0015408; F:ABC-type ferric iron transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR CDD; cd03259; ABC_Carb_Solutes_like; 1.
DR Gene3D; 2.40.50.140; -; 1.
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; IPR015853; ABC_transpr_FbpC.
DR InterPro; IPR040856; GlcV_C.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17847; GlcV_C_terminal; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 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; Nucleotide-binding;
KW Reference proteome; Sugar transport; Translocase; Transport.
FT CHAIN 1..353
FT /note="Glucose import ATP-binding protein GlcV"
FT /id="PRO_0000447615"
FT DOMAIN 4..241
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 40..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:12823973"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:12823973"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:12823973"
FT MUTAGEN 142
FT /note="S->A: Decrease in ATPase activity. Can form dimers."
FT /evidence="ECO:0000269|PubMed:14607117"
FT MUTAGEN 144
FT /note="G->A: Loss of ATPase activity. Cannot form dimers.
FT Forms an active heterodimer; when associated with A-166."
FT /evidence="ECO:0000269|PubMed:14607117"
FT MUTAGEN 166
FT /note="E->A: Loss of ATPase activity. Can form dimers in
FT the presence of ATP-Mg(2+). Forms an active heterodimer;
FT when associated with A-144."
FT /evidence="ECO:0000269|PubMed:14607117"
FT MUTAGEN 166
FT /note="E->Q: Strong decrease in ATPase activity. Can form
FT dimers in the presence of ATP alone, without Mg(2+)."
FT /evidence="ECO:0000269|PubMed:14607117"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:1OXX"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 293..307
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:1OXX"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1OXX"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:1OXX"
SQ SEQUENCE 353 AA; 39113 MW; 772D42F471DCD980 CRC64;
MVRIIVKNVS KVFKKGKVVA LDNVNINIEN GERFGILGPS GAGKTTFMRI IAGLDVPSTG
ELYFDDRLVA SNGKLIVPPE DRKIGMVFQT WALYPNLTAF ENIAFPLTNM KMSKEEIRKR
VEEVAKILDI HHVLNHFPRE LSGGQQQRVA LARALVKDPS LLLLDEPFSN LDARMRDSAR
ALVKEVQSRL GVTLLVVSHD PADIFAIADR VGVLVKGKLV QVGKPEDLYD NPVSIQVASL
IGEINELEGK VTNEGVVIGS LRFPVSVSSD RAIIGIRPED VKLSKDVIKD DSWILVGKGK
VKVIGYQGGL FRITITPLDS EEEIFTYSDH PIHSGEEVLV YVRKDKIKVF EKN
