PT1_MYCCT
ID PT1_MYCCT Reviewed; 573 AA.
AC P45617; Q2SSP3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:330508};
DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:330508};
GN Name=ptsI; OrderedLocusNames=MCAP_0233;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7703858; DOI=10.1002/pro.5560031125;
RA Zhu P.-P., Reizer J., Peterkofsky A.;
RT "Unique dicistronic operon (ptsI-crr) in Mycoplasma capricolum encoding
RT enzyme I and the glucose-specific enzyme IIA of the
RT phosphoenolpyruvate:sugar phosphotransferase system: cloning, sequencing,
RT promoter analysis, and protein characterization.";
RL Protein Sci. 3:2115-2128(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=783139; DOI=10.1128/jb.127.3.1298-1306.1976;
RA Ullah A.H., Cirillo V.P.;
RT "Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase system:
RT purification and characterization of the phosphocarrier protein.";
RL J. Bacteriol. 127:1298-1306(1976).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=330508; DOI=10.1128/jb.131.3.988-996.1977;
RA Jaffor Ullah A.H., Cirillo V.P.;
RT "Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase system:
RT purification and characterization of enzyme I.";
RL J. Bacteriol. 131:988-996(1977).
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 ECO:0000305|PubMed:330508}.
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};
CC -!- ACTIVITY REGULATION: Irreversibly inhibited the sulfhydryl reagent N-
CC ethylmaleimide (NEM). {ECO:0000269|PubMed:330508}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08839,
CC ECO:0000305|PubMed:330508}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:783139}.
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; U15110; AAA70406.1; -; Genomic_DNA.
DR EMBL; CP000123; ABC01377.1; -; Genomic_DNA.
DR RefSeq; WP_011387121.1; NC_007633.1.
DR AlphaFoldDB; P45617; -.
DR SMR; P45617; -.
DR EnsemblBacteria; ABC01377; ABC01377; MCAP_0233.
DR GeneID; 23778814; -.
DR KEGG; mcp:MCAP_0233; -.
DR HOGENOM; CLU_007308_7_0_14; -.
DR OMA; CNAEWAL; -.
DR OrthoDB; 467393at2; -.
DR PhylomeDB; P45617; -.
DR Proteomes; UP000001928; 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 Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphotransferase system;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..573
FT /note="Phosphoenolpyruvate-protein phosphotransferase"
FT /id="PRO_0000147075"
FT ACT_SITE 190
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 297
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 332
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 454..455
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 465
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
SQ SEQUENCE 573 AA; 64602 MW; 7F2951E4EEE0FEAD CRC64;
MSKQIKGIAA SEGISLARAL VIKETKLDIQ KQLISDVDQE IIKLEQAIEK SIADLKKIQQ
ITLKKLGEEK AAIFDAHQDI ANDPAIKEEV VELIKKEKVN AEYALFTVSN NYFEMFSQLE
DPYFKERSAD IKDVSLRIIS HILGLEIHDL STIDKEVIII SDDLTPSQTA QLDKKFVKGF
LTNVGGRTSH AAIMARSLEI PAILGLKNIT ELVKTDDLIA LDGSSGIVEL DLNDDDIKNY
QTKVQQYIEL KEQLKKFKDE PSLTKDKIKK LIEANIGSTN DVQSVLDSGA EGIGLFRTEF
LYMDNDHFPT EEEQFEAYKK VVSQIKHLVV FRTLDIGGDK KLSYFKFDEE MNPFLGYRAI
RFTLDRKDIF KDQIRALLRA SAFGKLGIMF PMIATIDEFK QAKTFVEECK IELDKEGIKY
DNQVQIGMMV EIPSAAILAD QFAKYADFFS IGTNDLIQYS FASDRMNQNV SYLYQPLNPS
LLRLIQLTIS GAHKHNKWVG MCGEMAGDSK ALPILLGLDL DAFSMSATSV LKARSLMSKI
EFSKAKILAN KVLECETNEQ VNKLVEDFLN NLD
