GLCS_SACS2
ID GLCS_SACS2 Reviewed; 554 AA.
AC Q97UZ1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Glucose-binding protein GlcS {ECO:0000305};
DE Short=GBP {ECO:0000303|PubMed:10400586};
GN Name=glcS {ECO:0000303|PubMed:11260467};
GN OrderedLocusNames=SSO2847 {ECO:0000312|EMBL:AAK42957.1};
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 PROTEIN SEQUENCE OF 13-43, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Part of the ABC transporter complex GlcSTUV involved in
CC glucose uptake (Probable). Binds glucose. Can also bind galactose and
CC mannose (PubMed:10400586, PubMed:11260467).
CC {ECO:0000269|PubMed:10400586, ECO:0000269|PubMed:11260467,
CC ECO:0000305|PubMed:10400586, ECO:0000305|PubMed:11260467}.
CC -!- ACTIVITY REGULATION: Binding of glucose is strongly inhibited by
CC galactose and mannose. {ECO:0000269|PubMed:10400586}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 1.5. {ECO:0000269|PubMed:10400586};
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). {ECO:0000305|PubMed:10400586}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10400586};
CC Multi-pass membrane protein {ECO:0000255}; Extracellular side
CC {ECO:0000305|PubMed:10400586}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AE006641; AAK42957.1; -; Genomic_DNA.
DR PIR; F90462; F90462.
DR RefSeq; WP_010923998.1; NC_002754.1.
DR AlphaFoldDB; Q97UZ1; -.
DR SMR; Q97UZ1; -.
DR STRING; 273057.SSO2847; -.
DR TCDB; 3.A.1.1.13; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAK42957; AAK42957; SSO2847.
DR GeneID; 27429113; -.
DR KEGG; sso:SSO2847; -.
DR PATRIC; fig|273057.12.peg.2932; -.
DR eggNOG; arCOG00150; Archaea.
DR HOGENOM; CLU_491464_0_0_2; -.
DR InParanoid; Q97UZ1; -.
DR OMA; NTPEQWW; -.
DR PhylomeDB; Q97UZ1; -.
DR Proteomes; UP000001974; 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:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR006059; SBP.
DR Pfam; PF01547; SBP_bac_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Glucose-binding protein GlcS"
FT /id="PRO_0000447612"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10400586"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..525
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:10400586"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..554
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10400586"
SQ SEQUENCE 554 AA; 61128 MW; 1A70B61AA280525C CRC64;
MKRKYPYSLA KGLTSTQIAV IVAVIVIVII IGVVAGFVLT KGPSTTAVTT TVTSTFTTTT
TIPSTTTSTP SNTVVFYTWW GGGDGGEALS QIIPAVKQYA GLQMQTYSIP GAGGTNAKYA
ILALIQAGKP PAAFQVHYGP EMISYVEAAP NGIHTFVNMT PYLIQWGLLN NAVYAVLQAG
AYNGTLLSVP INVHRGAVLY VNTQLLREYN LPFPYNFSTL VYDTVQLANH GVSPWIIPGG
DGGWDQFNVW EDIFLYLAGP QLYNELIYGT LNFSNPTVQK LINETNYWFL NFTSYNYPGW
QSMSWEQAFA LIAQGKVAFQ ANGNWVTNYA SYINVTVYPP LPQYISNSSV SVVETPFPGT
QHYYALVIDT IGIPVGPQEQ QALQLAHFWS SYQGQEVWTK YKAVTYYKNG TDWYAQPAQW
YDYQQLINTS EQNFVYQLSD GGVFDDVFAQ IDSGLLTLQQ VGKVGLSAWN STLVSSMQQE
QNEWLAAAKL GLGYLGFPGH PFAGYYPPWV TNPSAYGLTN NTQKTSNSVM LFLLPFLALP
LAIASIDNKY YLLK
