GLCP_STAES
ID GLCP_STAES Reviewed; 446 AA.
AC A0A0H2VG78;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Glucose transporter GlcP {ECO:0000305};
DE AltName: Full=Glucose/H(+) symporter {ECO:0000303|PubMed:24127585};
GN Name=glcP {ECO:0000303|PubMed:24127585};
GN OrderedLocusNames=SE_0247 {ECO:0000312|EMBL:AAO03844.1};
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
RN [2] {ECO:0007744|PDB:4LDS}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP MUTAGENESIS OF ASP-22; ARG-102; ILE-105; GLU-122; GLN-137; GLN-250;
RP GLN-251; ASN-256 AND TRP-357.
RX PubMed=24127585; DOI=10.1073/pnas.1311485110;
RA Iancu C.V., Zamoon J., Woo S.B., Aleshin A., Choe J.Y.;
RT "Crystal structure of a glucose/H+ symporter and its mechanism of action.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17862-17867(2013).
CC -!- FUNCTION: Transporter highly specific for glucose uptake.
CC {ECO:0000269|PubMed:24127585}.
CC -!- ACTIVITY REGULATION: Inhibited by carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP) and by the human glucose transport
CC inhibitors cytochalasin B, phloretin, and forskolin.
CC {ECO:0000269|PubMed:24127585}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for glucose {ECO:0000269|PubMed:24127585};
CC Vmax=160 nmol/min/mg enzyme {ECO:0000269|PubMed:24127585};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24127585};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24127585}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO03844.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE015929; AAO03844.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_763802.1; NC_004461.1.
DR RefSeq; WP_001830529.1; NC_004461.1.
DR PDB; 4LDS; X-ray; 3.20 A; A/B=1-446.
DR PDBsum; 4LDS; -.
DR AlphaFoldDB; A0A0H2VG78; -.
DR SMR; A0A0H2VG78; -.
DR STRING; 176280.SE_0247; -.
DR EnsemblBacteria; AAO03844; AAO03844; SE_0247.
DR GeneID; 50017642; -.
DR KEGG; sep:SE_0247; -.
DR PATRIC; fig|176280.10.peg.224; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_30_5_9; -.
DR Proteomes; UP000001411; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Sugar transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..446
FT /note="Glucose transporter GlcP"
FT /id="PRO_0000449125"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 32..38
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 39..64
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 65..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 91..94
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 95..122
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 123..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 153..154
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 155..180
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 181..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 235..269
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 270..272
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 296..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 325..329
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 330..363
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 364..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 371..399
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 400..401
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TRANSMEM 402..420
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24127585"
FT TOPO_DOM 421..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127585"
FT SITE 22
FT /note="Important for symport activity"
FT /evidence="ECO:0000305|PubMed:24127585"
FT SITE 105
FT /note="Important for symport activity"
FT /evidence="ECO:0000305|PubMed:24127585"
FT MUTAGEN 22
FT /note="D->N: Affects symport activity. May function as an
FT uniporter."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 102
FT /note="R->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 105
FT /note="I->S: Affects symport activity. May function as an
FT uniporter."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 122
FT /note="E->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 137
FT /note="Q->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 250
FT /note="Q->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 251
FT /note="Q->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 256
FT /note="N->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:24127585"
FT MUTAGEN 357
FT /note="W->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:24127585"
FT HELIX 8..32
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 41..60
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 72..88
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 96..123
FT /evidence="ECO:0007829|PDB:4LDS"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 133..151
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 157..179
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:4LDS"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:4LDS"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:4LDS"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:4LDS"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 280..296
FT /evidence="ECO:0007829|PDB:4LDS"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 304..326
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:4LDS"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:4LDS"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 370..390
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:4LDS"
FT HELIX 402..420
FT /evidence="ECO:0007829|PDB:4LDS"
SQ SEQUENCE 446 AA; 48375 MW; 6CCA6809FA493FE5 CRC64;
MKANKYLIFI LGALGGLLYG YDNGVISGAL LFIHKDIPLN STTEGIVVSS MLIGAIVGAG
SSGPLADKLG RRRLVMLIAI VFIIGALILA ASTNLALLII GRLIIGLAVG GSMSTVPVYL
SEMAPTEYRG SLGSLNQLMI TIGILAAYLV NYAFADIEGW RWMLGLAVVP SVILLVGIYF
MPESPRWLLE NRNEEAARQV MKITYDDSEI DKELKEMKEI NAISESTWTV IKSPWLGRIL
IVGCIFAIFQ QFIGINAVIF YSSSIFAKAG LGEAASILGS VGIGTINVLV TIVAIFVVDK
IDRKKLLVGG NIGMIASLLI MAILIWTIGI ASSAWIIIVC LSLFIVFFGI SWGPVLWVML
PELFPMRARG AATGISALVL NIGTLIVSLF FPILSDALST EWVFLIFAFI GVLAMIFVIK
FLPETRGRSL EEIEYELRER TGARTE
