CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002299
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable tRNA threonylcarbamoyladenosine biosynthesis protein Gcp 
Protein Synonyms/Alias
 t(6)A37 threonylcarbamoyladenosine biosynthesis protein 
Gene Name
 gcp 
Gene Synonyms/Alias
 ygjD; b3064; JW3036 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
64PLIQAALKESGLTAKacetylation[1]
171EAFDKTAKLLGLDYPacetylation[1]
185PGGPLLSKMAAQGTAacetylation[1]
261ALDQTGFKRLVMAGGacetylation[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
 Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. May also be involved in the metabolism of glycated proteins. 
Sequence Annotation
  
Keyword
 Complete proteome; Cytoplasm; Reference proteome; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 337 AA 
Protein Sequence
MRVLGIETSC DETGIAIYDD EKGLLANQLY SQVKLHADYG GVVPELASRD HVRKTVPLIQ 60
AALKESGLTA KDIDAVAYTA GPGLVGALLV GATVGRSLAF AWDVPAIPVH HMEGHLLAPM 120
LEDNPPEFPF VALLVSGGHT QLISVTGIGQ YELLGESIDD AAGEAFDKTA KLLGLDYPGG 180
PLLSKMAAQG TAGRFVFPRP MTDRPGLDFS FSGLKTFAAN TIRDNGTDDQ TRADIARAFE 240
DAVVDTLMIK CKRALDQTGF KRLVMAGGVS ANRTLRAKLA EMMKKRRGEV FYARPEFCTD 300
NGAMIAYAGM VRFKAGATAD LGVSVRPRWP LAELPAA 337 
Gene Ontology
 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0001948; F:glycoprotein binding; IDA:EcoCyc.
 GO:0042802; F:identical protein binding; IDA:EcoCyc.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0008233; F:peptidase activity; ISS:EcoCyc.
 GO:0070526; P:threonylcarbamoyladenosine biosynthetic process; IDA:EcoCyc. 
Interpro
 IPR000905; Gcp-like_dom.
 IPR017861; KAE1/YgjD.
 IPR017860; Peptidase_M22_CS.
 IPR022450; T6A_Gcp_(YgjD). 
Pfam
 PF00814; Peptidase_M22 
SMART
  
PROSITE
 PS01016; GLYCOPROTEASE 
PRINTS
 PR00789; OSIALOPTASE.