ID PTG3C_STAEQ Reviewed; 675 AA.
AC Q5HL73;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 01-MAY-2013, entry version 67.
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; OrderedLocusNames=SERP2114;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete
RT genome analysis of an early methicillin-resistant Staphylococcus
RT aureus strain and a biofilm-producing methicillin-resistant
RT Staphylococcus epidermidis strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW52991.1; -; Genomic_DNA.
DR RefSeq; YP_189670.1; NC_002976.3.
DR HSSP; P69786; 1O2F.
DR ProteinModelPortal; Q5HL73; -.
DR SMR; Q5HL73; 431-500.
DR STRING; 176279.SERP2114; -.
DR EnsemblBacteria; AAW52991; AAW52991; SERP2114.
DR GeneID; 3242483; -.
DR KEGG; ser:SERP2114; -.
DR PATRIC; 19615136; VBIStaEpi130894_2057.
DR eggNOG; COG1263; -.
DR HOGENOM; HOG000250993; -.
DR KO; K02763; -.
DR KO; K02764; -.
DR KO; K02765; -.
DR OMA; MESAGQI; -.
DR ProtClustDB; CLSK872840; -.
DR BioCyc; SEPI176279:GJJB-2191-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 1 675 PTS system glucose-specific EIICBA
FT component.
FT /FTId=PRO_0000351403.
FT TRANSMEM 16 36 Helical; (Potential).
FT TRANSMEM 59 79 Helical; (Potential).
FT TRANSMEM 81 101 Helical; (Potential).
FT TRANSMEM 126 146 Helical; (Potential).
FT TRANSMEM 170 190 Helical; (Potential).
FT TRANSMEM 211 231 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 378 398 Helical; (Potential).
FT DOMAIN 3 414 PTS EIIC type-1.
FT DOMAIN 425 506 PTS EIIB type-1.
FT DOMAIN 547 651 PTS EIIA type-1.
FT ACT_SITE 447 447 Phosphocysteine intermediate; for EIIB
FT activity (By similarity).
FT ACT_SITE 599 599 Tele-phosphohistidine intermediate; for
FT EIIA activity (By similarity).
SQ SEQUENCE 675 AA; 73359 MW; AD6EC55F6C15C4C2 CRC64;
MFKKLFGQMQ RIGKALMLPV AILPAAGLLL AIGTAFQGEA LQHYLPFIKN DIVQQIANML
TGAGGIIFDN LPIIFALGVA IGLAGGDGVA AIAAFVGFII LNKTMGAFLH VTPDKLSDPT
NGYANVLGIP TLQTGVFGGI IIGALAAWCY NKFYNITLPS YLGFFAGKRF VPIMMATTSF
ILAFPMAIIW PTIQNGLNAF SEGLLDSNTG LAVFLFGFIK RLLIPFGLHH IFHAPFWFEF
GSWKNAAGEI IRGDQRIFIE QIREGAHLTS GKFMQGEFPV MMFGLPAAAL AIYQTAKPEN
KKVVAGLMIS AALTSFLTGI TEPLEFSFLF VAPFLFVIHA VLDGLSFLTL YLLNVHLGYT
FSGGFIDYVL LGILPNKTAW WLVIPVGIIY AVIYYFVFRF LIVKFNYKTP GREDKKSSVT
TTSASQLPFD VLKAMGGKEN IKHLDACITR LRVEVNEKSK VDVAGLKSLG ASGVLEVGNN
MQAIFGPKSD QIKHDMAKII SGEITKPSET TIDEEVSDDP VHVEDIVETE IYAPGHGEII
PLSEVPDKVF SEKMMGDGIG FVPDSGEIVA PFDGTVKTIF PTKHAIGLES DSGVEVLIHI
GIDTVKLNGE GFESLVNTDE PVTQGQPLMK IDLEYLKEHA PSIITPVIIT NQEDKTLTIE
DVKQVDPGKA IMTIK
//
