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Q9CJ82 (PT1_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. 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:LL0118
ORF Names:L120628
OrganismLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifier272623 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length575 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.

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 – 575575Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147070

Sites

Active site1911Tele-phosphohistidine intermediate By similarity
Active site5061Proton donor By similarity
Metal binding4351Magnesium By similarity
Metal binding4591Magnesium By similarity
Binding site2981Substrate By similarity
Binding site3341Substrate By similarity
Binding site4351Substrate By similarity
Binding site4561Substrate; via carbonyl oxygen By similarity
Binding site4571Substrate; via amide nitrogen By similarity
Binding site4581Substrate By similarity
Binding site4591Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CJ82 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 13C64D09D76D8369

FASTA57562,561
        10         20         30         40         50         60 
MTTMLKGIAA SSGVAVAKAY LLVQPDLSFE TKTIADTANE EARLDAALAT SQSELQLIKD 

        70         80         90        100        110        120 
KAVTTLGEEA ASVFDAHMMV LADPDMTAQI KAVINDKKVN AESALKEVTD MFIGIFEGMT 

       130        140        150        160        170        180 
DNAYMQERAA DIKDVTKRVL AHLLGVKLPS PALIDEEVII VAEDLTPSDT AQLDKKFVKA 

       190        200        210        220        230        240 
FVTNIGGRTS HSAIMARTLE IPAVLGTNNI TELVSEGQLL AVSGLTGEVI LDPSTEQQSE 

       250        260        270        280        290        300 
FHKAGEAYAA QKAEWAALKD AETVTADGRH YELAANIGTP KDVEGVNDNG AEAIGLYRTE 

       310        320        330        340        350        360 
FLYMDAQDFP TEDDQYEAYK AVLEGMNGKP VVVRTMDIGG DKTLPYFDLP KEMNPFLGWR 

       370        380        390        400        410        420 
ALRISLSTAG DGMFRTQLRA LLRASVHGQL RIMFPMVALV TEFRAAKKIY DEEKAKLIAE 

       430        440        450        460        470        480 
GVPVADGIEV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP 

       490        500        510        520        530        540 
YNPSILRLIN NVIKAAHAEG KWAGMCGEMA GDQTAVPLLM GMGLDEFSMS ATSVLQTRSL 

       550        560        570 
MKRLDSKKME ELSSKALSEC ATMEEVIALV EEYTK

« Hide

References

[1]"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IL1403.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005176 Genomic DNA. Translation: AAK04216.1.
PIRF86639.
RefSeqNP_266274.1. NC_002662.1.

3D structure databases

ProteinModelPortalQ9CJ82.
SMRQ9CJ82. Positions 5-575.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1113724.
GenomeReviewsGene locus LL0118 in contig AE005176_GR.
KEGGlla:L120628.
NMPDRfig|272623.1.peg.125.
PATRIC22292388. VBILacLac136773_0132.

Phylogenomic databases

HOGENOMHBG456539.
OMAIFSAHLL.
ProtClustDBCLSK876691.

Enzyme and pathway databases

BioCycLLAC272623:L120628-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_LACLA
AccessionPrimary (citable) accession number: Q9CJ82
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 72 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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