ID PTU3C_STAA9 Reviewed; 688 AA.
AC A5IVW5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 53.
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=2.7.1.69;
DE AltName: Full=PTS system glucoside-specific EIIB component;
DE Includes:
DE RecName: Full=Glucoside-specific phosphotransferase enzyme IIA component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system glucoside-specific EIIA component;
GN Name=glcB; OrderedLocusNames=SaurJH9_2561;
OS Staphylococcus aureus (strain JH9).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=359786;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JH9;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT "Complete sequence of chromosome of Staphylococcus aureus subsp.
RT aureus JH9.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar
CC phosphotransferase system (sugar PTS), a major carbohydrate active
CC -transport system, catalyzes the phosphorylation of incoming sugar
CC substrates concomitantly with their translocation across the cell
CC membrane. This system is involved in alpha- and beta-glucoside
CC transport (By similarity).
CC -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC histidine/cysteine.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity).
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC and 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
CC histidyl residue. Then, it transfers the phosphoryl group to the
CC EIIB domain.
CC -!- SIMILARITY: Contains 1 PTS EIIA type-1 domain.
CC -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain.
CC -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain.
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DR EMBL; CP000703; ABQ50338.1; -; Genomic_DNA.
DR RefSeq; YP_001247914.1; NC_009487.1.
DR ProteinModelPortal; A5IVW5; -.
DR SMR; A5IVW5; 447-509.
DR STRING; 359786.SaurJH9_2561; -.
DR EnsemblBacteria; ABQ50338; ABQ50338; SaurJH9_2561.
DR GeneID; 5168664; -.
DR KEGG; saj:SaurJH9_2561; -.
DR PATRIC; 19543129; VBIStaAur42398_2703.
DR eggNOG; COG1263; -.
DR HOGENOM; HOG000250993; -.
DR KO; K02763; -.
DR KO; K02764; -.
DR KO; K02765; -.
DR OMA; FSDWAAH; -.
DR ProtClustDB; CLSK872840; -.
DR BioCyc; SAUR359786:GJEM-2643-MONOMER; -.
DR GO; GO:0016021; C:integral to 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:EC.
DR GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018113; PTrfase_EIIB/Cys_phosph_CS.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR001996; PTS_EIIB_1.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR011535; PTS_Glc-like_IIB_component.
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; Dup_hybrid_motif; 1.
DR SUPFAM; SSF55604; PTS_EIIB; 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; Complete proteome; Kinase; Membrane;
KW Phosphotransferase system; Sugar transport; Transferase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 688 PTS system glucoside-specific EIICBA
FT component.
FT /FTId=PRO_5000247418.
FT TRANSMEM 12 32 Helical; (Potential).
FT TRANSMEM 81 101 Helical; (Potential).
FT TRANSMEM 137 157 Helical; (Potential).
FT TRANSMEM 182 202 Helical; (Potential).
FT TRANSMEM 223 243 Helical; (Potential).
FT TRANSMEM 284 304 Helical; (Potential).
FT TRANSMEM 315 335 Helical; (Potential).
FT TRANSMEM 340 360 Helical; (Potential).
FT TRANSMEM 364 384 Helical; (Potential).
FT TRANSMEM 395 415 Helical; (Potential).
FT DOMAIN 3 427 PTS EIIC type-1.
FT DOMAIN 438 519 PTS EIIB type-1.
FT DOMAIN 560 664 PTS EIIA type-1.
FT ACT_SITE 460 460 Phosphocysteine intermediate; for EIIB
FT activity (By similarity).
FT ACT_SITE 612 612 Tele-phosphohistidine intermediate; for
FT EIIA activity (By similarity).
SQ SEQUENCE 688 AA; 74416 MW; 11D5CCB25833DD21 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 VDEKVTQGQP LMKVNLAYLK AHAPSIVTPM
IITNLENKEL VIEDVQDADP GKLIMTVK
//
