Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Multiphosphoryl transfer protein 2 |
Protein Synonyms/Alias | MTP 2; Protein H |
Gene Name | ptsA |
Gene Synonyms/Alias | frwA, yijH; OrderedLocusNames=b3947, JW5555 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 669 | NQAMACRTSLEVEHL | T | HTP | [1] | 670 | QAMACRTSLEVEHLL | S | HTP | [1] | |
Reference | [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M Mol. Cell Proteomics 2008, Feb;7(2):299-307. [ PMID:17938405] |
Functional Description From UniProt | FUNCTION: Multifunctional protein that includes general (non sugar-specific) and sugar-specific components 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). HPr transfers the phosphoryl group to the phosphoryl carrier EIIA, which then transfers it to EIIB (By similarity) |
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| Completeproteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphoprotein; Phosphotransferasesystem; Referenceproteome; Sugartransport; Transferase; Transport |
Protein Sequence | MALIVEFICE LPNGVHARPA SHVETLCNTF SSQIEWHNLR TDRKGNAKSA LALIGTDTLA 60 GDNCQLLISG ADEQEAHQRL SQWLRDEFPH CDAPLAEVKS DELEPLPVSL TNLNPQIIRA 120 RTVCSGSAGG ILTPISSLDL NALGNLPAAK GVDAEQSALE NGLTLVLKNI EFRLLDSDGA 180 TSAILEAHRS LAGDTSLREH LLAGVSAGLS CAEAIVASAN HFCEEFSRSS SSYLQERALD 240 VRDVCFQLLQ QIYGEQRFPA PGKLTQPAIC MADELTPSQF LELDKNHLKG LLLKSGGTTS 300 HTVILARSFN IPTLVGVDID ALTPWQQQTI YIDGNAGAIV VEPGEAVARY YQQEARVQDA 360 LREQQRVWLT QQARTADGIR IEIAANIAHS VEAQAAFGNG AEGVGLFRTE MLYMDRTSAP 420 GESELYNIFC QALESANGRS IIVRTMDIGG DKPVDYLNIP AEANPFLGYR AVRIYEEYAS 480 LFTTQLRSIL RASAHGSLKI MIPMISSMEE ILWVKEKLAE AKQQLRNEHI PFDEKIQLGI 540 MLEVPSVMFI IDQCCEEIDF FSIGSNDLTQ YLLAVDRDNA KVTRHYNSLN PAFLRALDYA 600 VQAVHRQGKW IGLCGELGAK GSVLPLLVGL GLDELSMSAP SIPAAKARMA QLDSRECRKL 660 LNQAMACRTS LEVEHLLAQF RMTQQDAPLV TAECITLESD WRSKEEVLKG MTDNLLLAGR 720 CRYPRKLEAD LWAREAVFST GLGFSFAIPH SKSEHIEQST ISVARLQAPV RWGDDEAQFI 780 IMLTLNKHAA GDQHMRIFSR LARRIMHEEF RNALVNAASA DAIASLLQHE LEL 833 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0016301 F:kinase activity IEA:UniProtKB-KW GO:0046872 F:metal ion binding IEA:UniProtKB-KW GO:0008965 F:phosphoenolpyruvate-protein phosphotransferase activity IEA:UniProtKB-EC GO:0005351 F:sugar:hydrogen symporter activity IEA:InterPro GO:0009401 P:phosphoenolpyruvate-dependent sugar phosphotransferase system IEA:UniProtKB-KW |
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