(data stored in ACNUC7421 zone)

HOGENOM: STAAS_1_PE1006

ID   STAAS_1_PE1006                       STANDARD;      PRT;   572 AA.
AC   STAAS_1_PE1006; Q6GAD0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phosphoenolpyruvate-protein phosphotransferase; EC=2.7.3
DE   9;AltName: Full=Phosphotransferase system, enzyme I; (STAAS_1.PE1006).
GN   OrderedLocusNames=SAS1019;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MSSA476.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAS_1.PE1006.
CC       Staphylococcus aureus subsp. aureus MSSA476 chromosome, complete genome
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PT1_STAAS
CC   -!- FUNCTION: General (non sugar-specific) component of the
CC       phosphoenolpyruvate-dependent sugar phosphotransferase system
CC       (sugar PTS). This major carbohydrate active-transport system
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane.
CC       Enzyme I transfers the phosphoryl group from phosphoenolpyruvate
CC       (PEP) to the phosphoryl carrier protein (HPr).
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + protein L-histidine =
CC       pyruvate + protein N(pi)-phospho-L-histidine.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The N-terminal domain contains the HPr binding site, the
CC       central domain the pyrophosphate/phosphate carrier histidine, and
CC       the C-terminal domain the pyruvate binding site (By similarity).
CC   -!- MISCELLANEOUS: The reaction takes place in three steps, mediated
CC       by a phosphocarrier histidine residue located on the surface of
CC       the central domain. The two first partial reactions are catalyzed
CC       at an active site located on the N-terminal domain, and the third
CC       partial reaction is catalyzed at an active site located on the C-
CC       terminal domain. For catalytic turnover, the central domain
CC       swivels from the concave surface of the N-terminal domain to that
CC       of the C-terminal domain (By similarity).
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC   -!- GENE_FAMILY: HOG000278513 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6GAD0; -.
DR   EMBL; BX571857; CAG42793.1; -; Genomic_DNA.
DR   RefSeq; YP_043143.1; NC_002953.3.
DR   ProteinModelPortal; Q6GAD0; -.
DR   SMR; Q6GAD0; 5-572.
DR   STRING; Q6GAD0; -.
DR   EnsemblBacteria; EBSTAT00000022897; EBSTAP00000022064; EBSTAG00000022896.
DR   GeneID; 2864072; -.
DR   GenomeReviews; BX571857_GR; SAS1019.
DR   KEGG; sas:SAS1019; -.
DR   eggNOG; COG1080; -.
DR   GeneTree; EBGT00050000024576; -.
DR   OMA; IFSAHLL; -.
DR   ProtClustDB; CLSK885128; -.
DR   BioCyc; SAUR282459:SAS1019-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein 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   InterPro; IPR008279; PEP-utiliz_enz_mobile_dom.
DR   InterPro; IPR006318; PEP_P_trans.
DR   InterPro; IPR018274; PEP_utiliser_AS.
DR   InterPro; IPR023151; PEP_utiliser_CS.
DR   InterPro; IPR000121; PEP_utilisers.
DR   InterPro; IPR008731; PTS_PEP_utilis_N.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase.
DR   Gene3D; G3DSA:3.50.30.10; PEP_mobile; 1.
DR   Gene3D; G3DSA:1.10.274.10; PTS_PEP_utilis_N; 1.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PRINTS; PR01736; PHPHTRNFRASE.
DR   SUPFAM; SSF47831; PEP-utilisers_N; 1.
DR   SUPFAM; SSF52009; PEP_mobile; 1.
DR   SUPFAM; SSF51621; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
DR   HOGENOMDNA; STAAS_1.PE1006; -.
KW   phosphoenolpyruvate-protein phosphotransferase;
KW   Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Phosphotransferase system; Sugar transport; Transferase; Transport.
SQ   SEQUENCE   572 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSKLIKGIAA SDGVAIAKAY LLVEPDLTFD KNEKVTDVEG EVAKFNSAIE ASKVELTKIR
     NNAEVQLGAD KAAIFDAHLL VLDDPELIQP IQDKIKNENA NAATALTDVT TQFVTIFESM
     DNEYMKERAA DIRDVSKRVL SHILGVELPN PSMIDESVVI VGNDLTPSDT AQLNKEFVQG
     FATNIGGRTS HSAIMSRSLE IPAIVGTKSI TQEVKQGDMI IVDGLNGDVI VNPTEDELIA
     YQDKRERYFA DKKELQKLRD ADTVTVDGVH AELAANIGTP NDLPGVIENG AQGIGLYRTE
     FLYMGRDQMP TEEEQFEAYK EVLEAMDGKR VVVRTLDIGG DKELSYLNLP EEMNPFLGYR
     AIRLCLAQQD IFRPQLRALL RASVYGKLNI MFPMVATINE FREAKAILLE EKENLKNEGH
     DISDDIELGI MVEIPATAAL ADVFAKEVDF FSIGTNDLIQ YTLAADRMSE RVSYLYQPYN
     PSILRLVKQV IEASHKEGKW TGMCGEMAGD ETAIPLLLGL GLDEFSMSAT SILKARRQIN
     GLSKNEMTEL ANRAVDCATQ EEVIELVNNY VK
//

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