PTU3C_STAA1
ID PTU3C_STAA1 Reviewed; 688 AA.
AC A7X6P1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=PTS system glucoside-specific EIICBA component;
DE Includes:
DE RecName: Full=Glucoside permease IIC component;
DE AltName: Full=PTS system glucoside-specific EIIC component;
DE Includes:
DE RecName: Full=Glucoside-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system glucoside-specific EIIB component;
DE Includes:
DE RecName: Full=Glucoside-specific phosphotransferase enzyme IIA component;
DE AltName: Full=PTS system glucoside-specific EIIA component;
GN Name=glcB; OrderedLocusNames=SAHV_2522;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active -transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system is involved in alpha- and beta-glucoside transport (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC cysteinyl or histidyl residue, depending on the transported sugar.
CC Then, it transfers the phosphoryl group to the sugar substrate
CC concomitantly with the sugar uptake processed by the EIIC domain.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
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DR EMBL; AP009324; BAF79405.1; -; Genomic_DNA.
DR RefSeq; WP_000473678.1; NC_009782.1.
DR AlphaFoldDB; A7X6P1; -.
DR SMR; A7X6P1; -.
DR KEGG; saw:SAHV_2522; -.
DR HOGENOM; CLU_012312_1_1_9; -.
DR OMA; YLIMTGT; -.
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:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 2.70.70.10; -; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR011299; PTS_IIBC_glc.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00830; PTBA; 1.
DR TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..688
FT /note="PTS system glucoside-specific EIICBA component"
FT /id="PRO_0000351407"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 3..427
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 438..519
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 560..664
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 460
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 612
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ SEQUENCE 688 AA; 74430 MW; 11D5C824835AFD21 CRC64;
MFKKLFGQLQ RIGKALMLPV AILPAAGILL AFGNAMHNEQ LVEIAPWLKN DIIVMISSVM
EAAGQVVFDN LPLLFAVGTA LGLAGGDGVA ALAALVGYLI MNATMGKVLH ITIDDIFSYA
KGAKELSQAA KEPAHALVLG IPTLQTGVFG GIIMGALAAW CYNKFYNITL PPFLGFFAGK
RFVPIVTSVV AIATGVLLSF AWPPIQDGLN SLSNFLLNKN LTLTTFIFGI IERSLIPFGL
HHIFYSPFWF EFGSYTNHAG ELVRGDQRIW MAQLKDGVPF TAGAFTTGKY PFMMFGLPAA
AFAIYKNARP ERKKVVGGLM LSAGLTAFLT GITEPLEFSF LFVAPVLYGI HVLLAGTSFL
VMHLLGVKIG MTFSGGFIDY ILYGLLNWDR SHALLVIPVG IVYAIVYYFL FDFAIRKFKL
KTPGREDEET EIRNSSVAKL PFDVLDAMGG KENIKHLDAC ITRLRVEVVD KSKVDVAGIK
ALGASGVLEV GNNMQAIFGP KSDQIKHDMA KIMSGEITKP SETTVTEEMS DEPVHVEALG
TTDIYAPGVG QIIPLSEVPD QVFAGKMMGD GIGFIPEKGE IVAPFDGTVK TIFPTKHAIG
LESESGVEVL IHIGIDTVKL NGEGFESLIN VDEKVTQAQP LMKVNLAYLK AHAPSIVTPM
IITNLENKEL VIEDVQDADP GKLIMTVK
