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P45617 (PT1_MYCCT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate-protein phosphotransferase
EC=2.7.3.9
Alternative name(s):
Phosphotransferase system, enzyme I
Gene names
Name:ptsI
Ordered Locus Names:MCAP_0233
OrganismMycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154) [Complete proteome] [HAMAP]
Taxonomic identifier340047 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length573 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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).

Catalytic activity

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Cofactor

Magnesium By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 573573Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147075

Sites

Active site1901Tele-phosphohistidine intermediate By similarity
Active site5021Proton donor By similarity
Metal binding4311Magnesium By similarity
Metal binding4551Magnesium By similarity
Binding site2971Substrate By similarity
Binding site3321Substrate By similarity
Binding site4311Substrate By similarity
Binding site4521Substrate; via carbonyl oxygen By similarity
Binding site4531Substrate; via amide nitrogen By similarity
Binding site4541Substrate By similarity
Binding site4551Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P45617 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7F2951E4EEE0FEAD

FASTA57364,602
        10         20         30         40         50         60 
MSKQIKGIAA SEGISLARAL VIKETKLDIQ KQLISDVDQE IIKLEQAIEK SIADLKKIQQ 

        70         80         90        100        110        120 
ITLKKLGEEK AAIFDAHQDI ANDPAIKEEV VELIKKEKVN AEYALFTVSN NYFEMFSQLE 

       130        140        150        160        170        180 
DPYFKERSAD IKDVSLRIIS HILGLEIHDL STIDKEVIII SDDLTPSQTA QLDKKFVKGF 

       190        200        210        220        230        240 
LTNVGGRTSH AAIMARSLEI PAILGLKNIT ELVKTDDLIA LDGSSGIVEL DLNDDDIKNY 

       250        260        270        280        290        300 
QTKVQQYIEL KEQLKKFKDE PSLTKDKIKK LIEANIGSTN DVQSVLDSGA EGIGLFRTEF 

       310        320        330        340        350        360 
LYMDNDHFPT EEEQFEAYKK VVSQIKHLVV FRTLDIGGDK KLSYFKFDEE MNPFLGYRAI 

       370        380        390        400        410        420 
RFTLDRKDIF KDQIRALLRA SAFGKLGIMF PMIATIDEFK QAKTFVEECK IELDKEGIKY 

       430        440        450        460        470        480 
DNQVQIGMMV EIPSAAILAD QFAKYADFFS IGTNDLIQYS FASDRMNQNV SYLYQPLNPS 

       490        500        510        520        530        540 
LLRLIQLTIS GAHKHNKWVG MCGEMAGDSK ALPILLGLDL DAFSMSATSV LKARSLMSKI 

       550        560        570 
EFSKAKILAN KVLECETNEQ VNKLVEDFLN NLD

« Hide

References

« Hide 'large scale' references
[1]"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."
Zhu P.-P., Reizer J., Peterkofsky A.
Protein Sci. 3:2115-2128(1994) [PubMed: 7703858] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: California kid / ATCC 27343 / NCTC 10154.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U15110 Genomic DNA. Translation: AAA70406.1.
CP000123 Genomic DNA. Translation: ABC01377.1.
RefSeqYP_424220.1. NC_007633.1.

3D structure databases

ProteinModelPortalP45617.
SMRP45617. Positions 252-572.
ModBaseSearch...

Protein-protein interaction databases

STRINGP45617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3828981.
GenomeReviewsGene locus MCAP_0233 in contig CP000123_GR.
KEGGmcp:MCAP_0233.
PATRIC20004931. VBIMycCap130493_0236.
TIGRMCAP_0233.

Phylogenomic databases

eggNOGCOG1080.
HOGENOMHBG456539.
OMAIFSAHLL.
PhylomeDBP45617.
ProtClustDBCLSK745717.

Enzyme and pathway databases

BioCycMCAP340047:MCAP_0233-MONOMER.

Family and domain databases

InterProIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_enz_I.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK08483.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_MYCCT
AccessionPrimary (citable) accession number: P45617
Secondary accession number(s): Q2SSP3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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