PT1_STAAU
ID PT1_STAAU Reviewed; 572 AA.
AC P51183;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:19801641};
DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:19801641};
GN Name=ptsI;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=305A;
RA Kravanja M., Engelmann R., Christiansen I., Hengstenberg W.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), COFACTOR, ACTIVE SITE, AND SUBUNIT.
RX PubMed=19801641; DOI=10.1074/jbc.m109.057612;
RA Oberholzer A.E., Schneider P., Siebold C., Baumann U., Erni B.;
RT "Crystal structure of enzyme I of the phosphoenolpyruvate sugar
RT phosphotransferase system in the dephosphorylated state.";
RL J. Biol. Chem. 284:33169-33176(2009).
CC -!- FUNCTION: General (non sugar-specific) component of the
CC phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar
CC PTS). This major carbohydrate active-transport system catalyzes the
CC phosphorylation of incoming sugar substrates concomitantly with their
CC translocation across the cell membrane. Enzyme I transfers the
CC phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl
CC carrier protein (HPr). {ECO:0000250|UniProtKB:P08839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000250|UniProtKB:P08839};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:19801641};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19801641}.
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 the
CC C-terminal domain the pyruvate binding site.
CC {ECO:0000250|UniProtKB:P08839}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC phosphocarrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the N-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the C-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the N-terminal domain to that of the C-terminal domain.
CC {ECO:0000250|UniProtKB:P08839}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; X93205; CAA63689.1; -; Genomic_DNA.
DR RefSeq; WP_000040054.1; NZ_WOUL01000005.1.
DR PDB; 2WQD; X-ray; 2.40 A; A=1-572.
DR PDBsum; 2WQD; -.
DR AlphaFoldDB; P51183; -.
DR SMR; P51183; -.
DR OMA; CNAEWAL; -.
DR BRENDA; 2.7.3.9; 3352.
DR EvolutionaryTrace; P51183; -.
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:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR024692; PTS_EI.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PIRSF; PIRSF000732; PTS_enzyme_I; 1.
DR SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Phosphotransferase system; Sugar transport; Transferase; Transport.
FT CHAIN 1..572
FT /note="Phosphoenolpyruvate-protein phosphotransferase"
FT /id="PRO_0000147085"
FT ACT_SITE 191
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000305|PubMed:19801641"
FT ACT_SITE 504
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 298
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 334
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 456..457
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 467
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 38..61
FT /evidence="ECO:0007829|PDB:2WQD"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 123..143
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:2WQD"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2WQD"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 235..256
FT /evidence="ECO:0007829|PDB:2WQD"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:2WQD"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 369..382
FT /evidence="ECO:0007829|PDB:2WQD"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 455..463
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 481..496
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:2WQD"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 514..520
FT /evidence="ECO:0007829|PDB:2WQD"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 532..540
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 544..554
FT /evidence="ECO:0007829|PDB:2WQD"
FT HELIX 560..568
FT /evidence="ECO:0007829|PDB:2WQD"
SQ SEQUENCE 572 AA; 63219 MW; 0CDF16F050CA83DE 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 EVLEAMGGKR 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
