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Phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9) (Phosphotransferase system, enzyme I)

 PT1_MYCCT               Reviewed;         573 AA.
P45617; Q2SSP3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
22-NOV-2017, entry version 117.
RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:330508};
EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:330508};
Name=ptsI; OrderedLocusNames=MCAP_0233;
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC
27343 / NCTC 10154).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=340047;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7703858; DOI=10.1002/pro.5560031125;
Zhu P.-P., Reizer J., Peterkofsky A.;
"Unique dicistronic operon (ptsI-crr) in Mycoplasma capricolum
encoding enzyme I and the glucose-specific enzyme IIA of the
phosphoenolpyruvate:sugar phosphotransferase system: cloning,
sequencing, promoter analysis, and protein characterization.";
Protein Sci. 3:2115-2128(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=California kid / ATCC 27343 / NCTC 10154;
Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C.,
Nierman W.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
SUBCELLULAR LOCATION.
PubMed=783139;
Ullah A.H., Cirillo V.P.;
"Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase
system: purification and characterization of the phosphocarrier
protein.";
J. Bacteriol. 127:1298-1306(1976).
[4]
FUNCTION, ENZYME REGULATION, AND SUBUNIT.
PubMed=330508;
Jaffor Ullah A.H., Cirillo V.P.;
"Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase
system: purification and characterization of enzyme I.";
J. Bacteriol. 131:988-996(1977).
-!- FUNCTION: General (non sugar-specific) component of the
phosphoenolpyruvate-dependent sugar phosphotransferase system
(sugar PTS). This major carbohydrate active-transport system
catalyzes the phosphorylation of incoming sugar substrates
concomitantly with their translocation across the cell membrane.
Enzyme I transfers the phosphoryl group from phosphoenolpyruvate
(PEP) to the phosphoryl carrier protein (HPr).
{ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:330508}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + protein L-histidine =
pyruvate + protein N(pi)-phospho-L-histidine.
{ECO:0000250|UniProtKB:P08839}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P08839};
-!- ENZYME REGULATION: Irreversibly inhibited the sulfhydryl reagent
N-ethylmaleimide (NEM). {ECO:0000269|PubMed:330508}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08839,
ECO:0000305|PubMed:330508}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:783139}.
-!- DOMAIN: The N-terminal domain contains the HPr binding site, the
central domain the pyrophosphate/phosphate carrier histidine, and
the C-terminal domain the pyruvate binding site.
{ECO:0000250|UniProtKB:P08839}.
-!- MISCELLANEOUS: The reaction takes place in three steps, mediated
by a phosphocarrier histidine residue located on the surface of
the central domain. The two first partial reactions are catalyzed
at an active site located on the N-terminal domain, and the third
partial reaction is catalyzed at an active site located on the C-
terminal domain. For catalytic turnover, the central domain
swivels from the concave surface of the N-terminal domain to that
of the C-terminal domain. {ECO:0000250|UniProtKB:P08839}.
-!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
{ECO:0000305}.
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EMBL; U15110; AAA70406.1; -; Genomic_DNA.
EMBL; CP000123; ABC01377.1; -; Genomic_DNA.
RefSeq; WP_011387121.1; NC_007633.1.
ProteinModelPortal; P45617; -.
SMR; P45617; -.
EnsemblBacteria; ABC01377; ABC01377; MCAP_0233.
GeneID; 23778814; -.
KEGG; mcp:MCAP_0233; -.
HOGENOM; HOG000278513; -.
KO; K08483; -.
OMA; CNAEWAL; -.
OrthoDB; POG091H00IL; -.
Proteomes; UP000001928; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
Gene3D; 1.10.274.10; -; 1.
InterPro; IPR008279; PEP-util_enz_mobile_dom.
InterPro; IPR018274; PEP_util_AS.
InterPro; IPR000121; PEP_util_C.
InterPro; IPR023151; PEP_util_CS.
InterPro; IPR036637; Phosphohistidine_dom_sf.
InterPro; IPR024692; PTS_EI.
InterPro; IPR006318; PTS_EI-like.
InterPro; IPR008731; PTS_EIN.
InterPro; IPR036618; PtsI_HPr-bd_sf.
InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
Pfam; PF05524; PEP-utilisers_N; 1.
Pfam; PF00391; PEP-utilizers; 1.
Pfam; PF02896; PEP-utilizers_C; 1.
PIRSF; PIRSF000732; PTS_enzyme_I; 1.
SUPFAM; SSF47831; SSF47831; 1.
SUPFAM; SSF51621; SSF51621; 1.
SUPFAM; SSF52009; SSF52009; 1.
TIGRFAMs; TIGR01417; PTS_I_fam; 1.
PROSITE; PS00742; PEP_ENZYMES_2; 1.
PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding;
Phosphotransferase system; Sugar transport; Transferase; Transport.
CHAIN 1 573 Phosphoenolpyruvate-protein
phosphotransferase.
/FTId=PRO_0000147075.
REGION 454 455 PEP binding.
{ECO:0000250|UniProtKB:P08839}.
ACT_SITE 190 190 Tele-phosphohistidine intermediate.
{ECO:0000250|UniProtKB:P08839}.
ACT_SITE 502 502 Proton donor.
{ECO:0000250|UniProtKB:P08839}.
METAL 431 431 Magnesium.
{ECO:0000250|UniProtKB:P08839}.
METAL 455 455 Magnesium.
{ECO:0000250|UniProtKB:P08839}.
BINDING 297 297 PEP. {ECO:0000250|UniProtKB:P23533}.
BINDING 332 332 PEP. {ECO:0000250|UniProtKB:P08839}.
BINDING 465 465 PEP. {ECO:0000250|UniProtKB:P23533}.
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


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