Tag | Content |
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CPLM ID | CPLM-010290 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional protein HldE |
Protein Synonyms/Alias | D-beta-D-heptose 7-phosphate kinase; D-beta-D-heptose 7-phosphotransferase; D-beta-D-heptose 1-phosphate adenosyltransferase |
Gene Name | hldE |
Gene Synonyms/Alias | rfaE; waaE; yqiF; b3052; JW3024 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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84 | DAARALSKSLADVNV | acetylation | [1] | 92 | SLADVNVKCDFVSVP | acetylation | [1] | 106 | PTHPTITKLRVLSRN | acetylation | [1] | 169 | QMIQLARKAGVPVLI | acetylation | [1] | 179 | VPVLIDPKGTDFERY | acetylation | [1, 2] | 341 | AARKRGEKVVMTNGV | acetylation | [1] | 381 | VNSDASTKRLKGDSR | acetylation | [1] | 431 | ILPDLLVKGGDYKPE | acetylation | [1] | 436 | LVKGGDYKPEEIAGS | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] [2] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y. Mol Cell Proteomics. 2009 Feb;8(2):215-25. [ PMID: 18723842] |
Functional Description | Catalyzes the phosphorylation of D-glycero-D-manno- heptose 7-phosphate at the C-1 position to form D,D-heptose-1,7- bisphosphate. |
Sequence Annotation | NP_BIND 195 198 ATP (Potential). REGION 1 318 Ribokinase. REGION 344 477 Cytidylyltransferase. ACT_SITE 264 264 Potential. MOD_RES 179 179 N6-acetyllysine. |
Keyword | Acetylation; ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; Lipopolysaccharide biosynthesis; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 477 AA |
Protein Sequence | MKVTLPEFER AGVMVVGDVM LDRYWYGPTS RISPEAPVPV VKVNTIEERP GGAANVAMNI 60 ASLGANARLV GLTGIDDAAR ALSKSLADVN VKCDFVSVPT HPTITKLRVL SRNQQLIRLD 120 FEEGFEGVDP QPLHERINQA LSSIGALVLS DYAKGALASV QQMIQLARKA GVPVLIDPKG 180 TDFERYRGAT LLTPNLSEFE AVVGKCKTEE EIVERGMKLI ADYELSALLV TRSEQGMSLL 240 QPGKAPLHMP TQAQEVYDVT GAGDTVIGVL AATLAAGNSL EEACFFANAA AGVVVGKLGT 300 STVSPIELEN AVRGRADTGF GVMTEEELKL AVAAARKRGE KVVMTNGVFD ILHAGHVSYL 360 ANARKLGDRL IVAVNSDAST KRLKGDSRPV NPLEQRMIVL GALEAVDWVV SFEEDTPQRL 420 IAGILPDLLV KGGDYKPEEI AGSKEVWANG GEVLVLNFED GCSTTNIIKK IQQDKKG 477 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:HAMAP. GO:0033785; F:heptose 7-phosphate kinase activity; IDA:EcoCyc. GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IDA:EcoCyc. GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway. |
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