CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
84DAARALSKSLADVNVacetylation[1]
92SLADVNVKCDFVSVPacetylation[1]
106PTHPTITKLRVLSRNacetylation[1]
169QMIQLARKAGVPVLIacetylation[1]
179VPVLIDPKGTDFERYacetylation[1, 2]
341AARKRGEKVVMTNGVacetylation[1]
381VNSDASTKRLKGDSRacetylation[1]
431ILPDLLVKGGDYKPEacetylation[1]
436LVKGGDYKPEEIAGSacetylation[1]
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. 
Interpro
 IPR023030; Bifunc_HldE.
 IPR002173; Carboh/pur_kinase_PfkB_CS.
 IPR004821; Cyt_trans-like.
 IPR011611; PfkB_dom.
 IPR011913; RfaE_dom_I.
 IPR011914; RfaE_dom_II.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF01467; CTP_transf_2
 PF00294; PfkB 
SMART
  
PROSITE
 PS00583; PFKB_KINASES_1
 PS00584; PFKB_KINASES_2 
PRINTS