CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002930
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GTPase Der 
Protein Synonyms/Alias
 Double era-like domain protein; GTP-binding protein EngA 
Gene Name
 der 
Gene Synonyms/Alias
 engA; yfgK; b2511; JW5403 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
104PADEAIAKHLRSREKacetylation[1]
272KITDAVEKFSVIKTLacetylation[1]
331DGLSQEVKEQVKETLacetylation[1]
335QEVKEQVKETLDFRLacetylation[1]
408RGRRVKLKYAHAGGYacetylation[1]
428VIHGNQVKDLPDSYKacetylation[1]
444YLMNYFRKSLDVMGSacetylation[1]
458SPIRIQFKEGENPYAacetylation[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
Functional Description
 GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a very late stage of 50S subunit maturation possibly by interacting with 23S rRNA or 23S rRNA/r-protein complex. 
Sequence Annotation
 DOMAIN 14 119 G 1.
 DOMAIN 214 322 G 2.
 DOMAIN 376 461 KH-like.
 NP_BIND 9 16 GTP 1 (Potential).
 NP_BIND 56 60 GTP 1 (Potential).
 NP_BIND 118 121 GTP 1 (Potential).
 NP_BIND 209 216 GTP 2 (Potential).
 NP_BIND 256 260 GTP 2 (Potential).
 NP_BIND 321 324 GTP 2 (Potential).  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome; Repeat; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 490 AA 
Protein Sequence
MVPVVALVGR PNVGKSTLFN RLTRTRDALV ADFPGLTRDR KYGRAEIEGR EFICIDTGGI 60
DGTEDGVETR MAEQSLLAIE EADVVLFMVD ARAGLMPADE AIAKHLRSRE KPTFLVANKT 120
DGLDPDQAVV DFYSLGLGEI YPIAASHGRG VLSLLEHVLL PWMEDLAPQE EVDEDAEYWA 180
QFEAEENGEE EEEDDFDPQS LPIKLAIVGR PNVGKSTLTN RILGEERVVV YDMPGTTRDS 240
IYIPMERDGR EYVLIDTAGV RKRGKITDAV EKFSVIKTLQ AIEDANVVML VIDAREGISD 300
QDLSLLGFIL NSGRSLVIVV NKWDGLSQEV KEQVKETLDF RLGFIDFARV HFISALHGSG 360
VGNLFESVRE AYDSSTRRVG TSMLTRIMTM AVEDHQPPLV RGRRVKLKYA HAGGYNPPIV 420
VIHGNQVKDL PDSYKRYLMN YFRKSLDVMG SPIRIQFKEG ENPYANKRNT LTPTQMRKRK 480
RLMKHIKKNK 490 
Gene Ontology
 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IDA:EcoCyc.
 GO:0043022; F:ribosome binding; IDA:EcoCyc.
 GO:0000027; P:ribosomal large subunit assembly; IMP:EcoCyc. 
Interpro
 IPR016484; GTP-bd_EngA.
 IPR006073; GTP_binding_domain.
 IPR015946; KH_dom-like_a/b.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom. 
Pfam
 PF01926; MMR_HSR1 
SMART
  
PROSITE
  
PRINTS
 PR00326; GTP1OBG.