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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 |
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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
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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
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Structure: | |
[...more] |
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Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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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