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8.A.7.1.1
Enzyme I of the PTS

Accession Number:P08839
Protein Name:PT1 aka PTSI aka B2416
Length:575
Molecular Weight:63562.00
Species:Escherichia coli [83333]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate

Cross database links:

DIP: DIP-10603N
RefSeq: AP_003010.1    NP_416911.1   
Entrez Gene ID: 946879   
Pfam: PF05524    PF00391    PF02896   
BioCyc: EcoCyc:PTSI-MONOMER    ECOL168927:B2416-MONOMER   
KEGG: ecj:JW2409    eco:b2416   

Gene Ontology

GO:0005829 C:cytosol
GO:0016301 F:kinase activity
GO:0046872 F:metal ion binding
GO:0008965 F:phosphoenolpyruvate-protein phosphotransfer...
GO:0005515 F:protein binding
GO:0005351 F:sugar:hydrogen symporter activity
GO:0009401 P:phosphoenolpyruvate-dependent sugar phospho...
GO:0016310 P:phosphorylation

References (14)

[1] “The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription.”  de Reuse H.et.al.   2457575
[2] “Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes.”  Saffen D.W.et.al.   2960675
[3] “Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.”  Yamamoto Y.et.al.   9205837
[4] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[5] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[6] “Analysis of the ptsH-ptsI-crr region in Escherichia coli K-12: nucleotide sequence of the ptsH gene.”  de Reuse H.et.al.   2411636
[7] “DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH.”  Byrne C.R.et.al.   3290198
[8] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[9] “Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant.”  Powell B.S.et.al.   7876255
[10] “The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr.”  Liao D.-I.et.al.   8805571
[11] “Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.”  Garrett D.S.et.al.   9054557
[12] “Tautomeric state and pKa of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system.”  Garrett D.S.et.al.   9541412
[13] “Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.”  Garrett D.S.et.al.   10048929
[14] “Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein.”  Teplyakov A.et.al.   17053069
Structure:
1EZA   1EZB   1EZC   1EZD   1ZYM   2EZA   2EZB   2EZC   2HWG   3EZA   [...more]

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FASTA formatted sequence
1:	MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK 
61:	AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD 
121:	EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI 
181:	TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR 
241:	AVQEQVASEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL 
301:	FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAI 
361:	RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF 
421:	DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS 
481:	VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT 
541:	NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKTIC