PT1_STACT
ID PT1_STACT Reviewed; 573 AA.
AC P23533; B9DQ26;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:1551842};
DE EC=2.7.3.9 {ECO:0000269|PubMed:1551842};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:1551842};
GN Name=ptsI; OrderedLocusNames=Sca_0705;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=1551842; DOI=10.1128/jb.174.7.2208-2214.1992;
RA Kohlbrecher D., Eisermann R., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system:
RT molecular cloning and nucleotide sequence of the Staphylococcus carnosus
RT ptsI gene and expression and complementation studies of the gene product.";
RL J. Bacteriol. 174:2208-2214(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
RX PubMed=1901791; DOI=10.1111/j.1432-1033.1991.tb15875.x;
RA Eisermann R., Fischer R., Kessler U., Neubauer A., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system.
RT Purification and protein sequencing of the Staphylococcus carnosus
RT histidine-containing protein, and cloning and DNA sequencing of the ptsH
RT gene.";
RL Eur. J. Biochem. 197:9-14(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=16867985; DOI=10.1074/jbc.m513721200;
RA Marquez J., Reinelt S., Koch B., Engelmann R., Hengstenberg W.,
RA Scheffzek K.;
RT "Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent
RT sugar phosphotransferase system.";
RL J. Biol. Chem. 281:32508-32515(2006).
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:0000269|PubMed:1551842}.
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:0000269|PubMed:1551842};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:1551842};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 uM for PEP {ECO:0000269|PubMed:1551842};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16867985}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; M69050; AAA26664.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL27616.1; -; Genomic_DNA.
DR EMBL; X60766; CAA43176.1; -; Genomic_DNA.
DR PIR; B42374; B42374.
DR RefSeq; WP_015899959.1; NC_012121.1.
DR PDB; 2HRO; X-ray; 2.50 A; A=1-573.
DR PDBsum; 2HRO; -.
DR AlphaFoldDB; P23533; -.
DR SMR; P23533; -.
DR STRING; 396513.SCA_0705; -.
DR GeneID; 60545595; -.
DR KEGG; sca:SCA_0705; -.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_7_0_9; -.
DR OMA; CNAEWAL; -.
DR OrthoDB; 467393at2; -.
DR BioCyc; SCAR396513:SCA_RS03580-MON; -.
DR BRENDA; 2.7.3.9; 5873.
DR SABIO-RK; P23533; -.
DR EvolutionaryTrace; P23533; -.
DR Proteomes; UP000000444; Chromosome.
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..573
FT /note="Phosphoenolpyruvate-protein phosphotransferase"
FT /id="PRO_0000147087"
FT ACT_SITE 190
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000305|PubMed:16867985"
FT ACT_SITE 503
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000305|PubMed:16867985"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16867985"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16867985"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 455..456
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:16867985"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16867985"
FT CONFLICT 124
FT /note="M -> I (in Ref. 1; AAA26664)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> AK (in Ref. 1; AAA26664)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..420
FT /note="LLEEERANLKNEGYE -> FLKKNVLTLKMKAMK (in Ref. 1;
FT AAA26664)"
FT /evidence="ECO:0000305"
FT CONFLICT 479..484
FT /note="NPAILR -> ISNFSF (in Ref. 1; AAA26664)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="R -> V (in Ref. 1; AAA26664)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 37..66
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 124..143
FT /evidence="ECO:0007829|PDB:2HRO"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:2HRO"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:2HRO"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:2HRO"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:2HRO"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 397..415
FT /evidence="ECO:0007829|PDB:2HRO"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 480..495
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:2HRO"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 513..519
FT /evidence="ECO:0007829|PDB:2HRO"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 543..553
FT /evidence="ECO:0007829|PDB:2HRO"
FT HELIX 559..569
FT /evidence="ECO:0007829|PDB:2HRO"
SQ SEQUENCE 573 AA; 63299 MW; EB31B4DB01D0611D CRC64;
MAKQIKGIAA SDGVAIAKAY LLVEPDLSFD NESVTDTDAE VAKFNGALNK SKVELTKIRN
NAEKQLGADK AAIFDAHLLV LEDPELIQPI EDKIKNESVN AAQALTDVSN QFITIFESMD
NEYMAERAAD IRDVSKRVLA HILGVELPNP SIVDESVVII GNDLTPSDTA QLNKEYVQGF
VTNIGGRTSH SAIMSRSLEI PAVVGTKSIT EEVEAGDTIV VDGMTGDVLI NPSDEVIAEY
QEKRENFFKD KQELQKLRDA ESVTADGHHV ELAANIGTPN DLPGVIENGA EGIGLYRTEF
LYMGRDQMPT EEEQFEAYKA VLEAMKGKRV VVRTLDIGGD KELPYLDLPE EMNPFLGYRA
IRLCLDQPEI FRPQLRALLR ASVFGKLNIM FPMVATIQEF RDAKALLEEE RANLKNEGYE
VADDIELGIM VEIPSTAALA DIFAKEVDFF SIGTNDLIQY TMAADRMSER VSYLYQPYNP
AILRLVKQVI EASHAEGKWT GMCGEMAGDQ TAIPLLLGLG LDEFSMSATS ILKARRLIRS
LNESEMKELS ERAVQCATSE EVVDLVEEYT KNA
