Phosphoenolpyruvate-protein phosphotransferase

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O31149 (PT1_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate-protein phosphotransferase
EC=2.7.3.9

Alternative name(s):
Phosphotransferase system, enzyme I

Gene names

Name:	ptsI
Ordered Locus Names:	lmo1003

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Protein existence	Inferred 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) By similarity.
Catalytic activity	Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subcellular location	Cytoplasm By similarity.
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.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-protein phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 572

572

Phosphoenolpyruvate-protein phosphotransferase

PRO_0000147074

Sites

Active site

190

Tele-phosphohistidine intermediate By similarity

Active site

503

Proton donor By similarity

Metal binding

432

Magnesium By similarity

Metal binding

456

Magnesium By similarity

Binding site

297

Substrate By similarity

Binding site

333

Substrate By similarity

Binding site

432

Substrate By similarity

Binding site

453

Substrate; via carbonyl oxygen By similarity

Binding site

454

Substrate; via amide nitrogen By similarity

Binding site

455

Substrate By similarity

Binding site

456

Substrate; via amide nitrogen By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O31149 [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 801CF440DE56EF06
Show »

FASTA

572

63,212

        10         20         30         40         50         60 
MAKELKGIAA SDGIAIAKAY LLVEPDLSYE KTEVTDVESE VKRFESALEV SRTELSMIRE 

        70         80         90        100        110        120 
KAAKDLGEDK AQIFDAHLLV LNDPELTGPI EESIKNSKTN AETALQETTD MFIGMFESMD 

       130        140        150        160        170        180 
NEYMRERAAD IKDVRKRVLS HLLGVTIPNP ALIDEEVVVV AADLTPSDTA QLNRNFVKGF 

       190        200        210        220        230        240 
VTDIGGRTSH SAIMARSLEI PAVVGTKEVT ASVAKNDIVI IDGLEGNVII HPTEEQIAHY 

       250        260        270        280        290        300 
EKIKSDFALQ QAEWDKLKNE KTVSKDGVHV ELAANIGTPN DLEGVISNGG EAVGLYRTEF 

       310        320        330        340        350        360 
LYMGRDNFPT EEEQFEAYKA VVSGMDGKSV VVRTLDIGGD KTLPYLELPE EMNPFLGFRA 

       370        380        390        400        410        420 
IRLCFANEEL FRTQLRALLR ASVYGNLKIM FPMIATVNEF RQARDILLDE KAKLKAAGTE 

       430        440        450        460        470        480 
VSDSIELGIM IEIPAAAVLA DQFAKEVDFF SIGTNDLIQY TMAADRMNER VSYLYQPYNP 

       490        500        510        520        530        540 
SILRLVKMVI DASHKEGKWT GMCGEMAGDQ TAVPLLLGLG LDEFSMSASS ILKSRSLIKR 

       550        560        570 
LDQSEMVKLA EEALNKSTAE EVVELVEKYT AE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.
[2]	"Cloning and expression of the Listeria monocytogenes Scott A ptsH and ptsI genes, coding for HPr and enzyme I, respectively, of the phosphotransferase system." Christensen D.P., Benson A.K., Hutkins R.W. Appl. Environ. Microbiol. 64:3147-3152(1998) [PubMed: 9726852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-509. Strain: Scott A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591977 Genomic DNA. Translation: CAC99081.1. AF030824 Genomic DNA. Translation: AAC36128.1.
PIR	AC1200.
RefSeq	NP_464528.1. NC_003210.1.
3D structure databases
ProteinModelPortal	O31149.
SMR	O31149. Positions 4-570.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	986170.
GenomeReviews	Gene locus lmo1003 in contig AL591824_GR.
KEGG	lmo:lmo1003.
PATRIC	20311106. VBILisMon69206_1031.
Organism-specific databases
GenoList	LMO1003.
Phylogenomic databases
HOGENOM	HBG456539.
OMA	IFSAHLL.
ProtClustDB	CLSK564210.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1003-MONOMER.
Family and domain databases
InterPro	IPR008279. 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]
Gene3D	G3DSA: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.
KO	K08483.
PANTHER	PTHR22931:SF10. PTHR22931:SF10. 1 hit.
Pfam	PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view]
PIRSF	PIRSF000732. PTS_enzyme_I. 1 hit.
PRINTS	PR01736. PHPHTRNFRASE.
SUPFAM	SSF47831. PEP-utilisers_N. 1 hit. SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01417. PTS_I_fam. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PT1_LISMO

Accession

Primary (citable) accession number: O31149

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 5, 2001
Last modified:	January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents