ID PTG3C_STAA9 Reviewed; 681 AA.
AC A5IP58;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=PTS system glucose-specific EIICBA component;
DE AltName: Full=EIICBA-Glc;
DE Short=EII-Glc;
DE Includes:
DE RecName: Full=Glucose permease IIC component;
DE AltName: Full=PTS system glucose-specific EIIC component;
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.69;
DE AltName: Full=PTS system glucose-specific EIIB component;
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIA component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system glucose-specific EIIA component;
GN Name=ptsG; Synonyms=glcA; OrderedLocusNames=SaurJH9_0174;
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 glucose transport (By
CC 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; ABQ47981.1; -; Genomic_DNA.
DR RefSeq; YP_001245557.1; NC_009487.1.
DR ProteinModelPortal; A5IP58; -.
DR SMR; A5IP58; 430-498, 529-681.
DR STRING; 359786.SaurJH9_0174; -.
DR PRIDE; A5IP58; -.
DR EnsemblBacteria; ABQ47981; ABQ47981; SaurJH9_0174.
DR GeneID; 5167479; -.
DR KEGG; saj:SaurJH9_0174; -.
DR PATRIC; 19538012; VBIStaAur42398_0217.
DR eggNOG; COG1263; -.
DR HOGENOM; HOG000250993; -.
DR KO; K02763; -.
DR KO; K02764; -.
DR KO; K02765; -.
DR OMA; MESAGQI; -.
DR ProtClustDB; CLSK872840; -.
DR BioCyc; SAUR359786:GJEM-173-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 1 681 PTS system glucose-specific EIICBA
FT component.
FT /FTId=PRO_5000247134.
FT TRANSMEM 16 36 Helical; (Potential).
FT TRANSMEM 73 93 Helical; (Potential).
FT TRANSMEM 126 146 Helical; (Potential).
FT TRANSMEM 170 190 Helical; (Potential).
FT TRANSMEM 199 219 Helical; (Potential).
FT TRANSMEM 273 293 Helical; (Potential).
FT TRANSMEM 303 323 Helical; (Potential).
FT TRANSMEM 328 348 Helical; (Potential).
FT TRANSMEM 355 375 Helical; (Potential).
FT TRANSMEM 383 403 Helical; (Potential).
FT DOMAIN 3 414 PTS EIIC type-1.
FT DOMAIN 425 506 PTS EIIB type-1.
FT DOMAIN 551 655 PTS EIIA type-1.
FT ACT_SITE 447 447 Phosphocysteine intermediate; for EIIB
FT activity (By similarity).
FT ACT_SITE 603 603 Tele-phosphohistidine intermediate; for
FT EIIA activity (By similarity).
SQ SEQUENCE 681 AA; 73958 MW; 040ADA543CF31520 CRC64;
MRKKLFGQLQ RIGKALMLPV AILPAAGLLL AIGTAIQGEA LQHYLPFIQN GGVQNVAKLM
TAAGSIIFEN LPMIFALGVA IGLAGGDGVA AIAAFVGYII MNKTMGDFLQ VTPKNVTDPA
SGYASILGIP TLQTGVFGGI IIGALAAWCY NKFYNINLPS YLGFFAGKRF VPIMMATTSF
ILAFPMALIW PTIQSGLNAF STGLLDSNTG VAVFLFGFIK RLLIPFGLHH IFHAPFWFEF
GSWKNAAGEI IHGDQRIFIE QIREGAHLTA GKFMQGEFPV MMFGLPAAAL AIYHTAKPEN
KKVVAGLMGS AALTSFLTGI TEPLEFSFLF VAPLLFFIHA VLDGLSFLTL YLLDVHLGYT
FSGGFIDYVL LGVLPNKTQW WLVIPVGLVY AVIYYFVFRF LIVKLKYKTP GREDKQSQAV
TASATELPYA VLEAMGGKAN IKHLDACITR LRVEVNDKSK VDVPGLKDLG ASGVLEVGNN
MQAIFGPKSD QIKHEMQQIM NGQVVENPTT MEDDKDETVV VAEDKSATSE LSHIVHAPLT
GEVTPLSEVP DQVFSEKMMG DGIAIKPSQG EVRAPFNGKI QMIFPTKHAI GLVSDSGLEL
LIHIGLDTVK LNGEGFTLHV EEGQEVKQGD LLINFDLDYI RNHAKSDITP IIVTQGNITN
LDFKQGEHGN ISFGDQLFEA K
//
