CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003002
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome-binding factor A 
Protein Synonyms/Alias
 Protein P15B 
Gene Name
 rbfA 
Gene Synonyms/Alias
 P15B; yhbB; b3167; JW3136 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
17RVAQEMQKEIALILQacetylation[1]
60YVTFLNDKDEDAVKAacetylation[1]
66DKDEDAVKAGIKALQacetylation[1]
70DAVKAGIKALQEASGacetylation[1]
85FIRSLLGKAMRLRIVacetylation[1]
118NLVTSVVKHDEERRVacetylation[1]
131RVNPDDSKED*****acetylation[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
 Essential for efficient processing of 16S rRNA. Probably part of the 30S subunit prior to or during the final step in the processing of 16S free 30S ribosomal subunits. Could be some accessory protein needed for efficient assembly of the 30S subunit. May interact with the 5'-terminal helix region of 16S rRNA. Has affinity for free ribosomal 30S subunits but not for 70S ribosomes. Overexpression suppresses a cold-sensitive C23U 16S rRNA mutation and rimM deletion mutants. Its function probably overlaps Era. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Reference proteome; Ribosome biogenesis; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 133 AA 
Protein Sequence
MAKEFGRPQR VAQEMQKEIA LILQREIKDP RLGMMTTVSG VEMSRDLAYA KVYVTFLNDK 60
DEDAVKAGIK ALQEASGFIR SLLGKAMRLR IVPELTFFYD NSLVEGMRMS NLVTSVVKHD 120
EERRVNPDDS KED 133 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030490; P:maturation of SSU-rRNA; IMP:EcoliWiki. 
Interpro
 IPR015946; KH_dom-like_a/b.
 IPR000238; Ribosome-bd_facA.
 IPR023799; Ribosome-bd_facA_dom.
 IPR020053; Ribosome-bd_factorA_CS. 
Pfam
 PF02033; RBFA 
SMART
  
PROSITE
 PS01319; RBFA 
PRINTS