CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007125
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative ribosome biogenesis GTPase RsgA 
Protein Synonyms/Alias
  
Gene Name
 rsgA 
Gene Synonyms/Alias
 engC; yjeQ; b4161; JW4122 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
28RLKTSKEKPDYDDNLacetylation[1]
85RVVWRPGKPAAEGVNacetylation[1]
94AAEGVNVKGIVEAVHacetylation[1]
199SHTQDGLKPLEEALTacetylation[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
 May play a role in 30S ribosomal subunit biogenesis. Unusual circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover. Dispensible for viability, but important for overall fitness. The intrinsic GTPase activity is stimulated by the presence of 30S (160-fold increase in kcat) or 70S (96 fold increase in kcat) ribosomes (PubMed:14973029). The GTPase is inhibited by aminoglycoside antibiotics such as neomycin and paromycin (PubMed:15466596) streptomycin and spectinomycin (PubMed:15828870). This inhibition is not due to competition for binding sites on the 30S or 70S ribosome (PubMed:15828870). 
Sequence Annotation
 DOMAIN 121 271 EngC GTPase.
 NP_BIND 160 163 GTP (By similarity).
 NP_BIND 214 222 GTP (By similarity).
 REGION 1 113 Necessary for association with the
 REGION 1 20 Necessary for GMP-PNP-dependent
 MOTIF 297 310 Knuckle-like cysteine cluster.
 METAL 297 297 Zinc (By similarity).
 METAL 302 302 Zinc (By similarity).
 METAL 304 304 Zinc (By similarity).
 METAL 310 310 Zinc (By similarity).  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 350 AA 
Protein Sequence
MSKNKLSKGQ QRRVNANHQR RLKTSKEKPD YDDNLFGEPD EGIVISRFGM HADVESADGD 60
VHRCNIRRTI RSLVTGDRVV WRPGKPAAEG VNVKGIVEAV HERTSVLTRP DFYDGVKPIA 120
ANIDQIVIVS AILPELSLNI IDRYLVACET LQIEPIIVLN KIDLLDDEGM AFVNEQMDIY 180
RNIGYRVLMV SSHTQDGLKP LEEALTGRIS IFAGQSGVGK SSLLNALLGL QKEILTNDIS 240
DNSGLGQHTT TAARLYHFPH GGDVIDSPGV REFGLWHLEP EQITQGFVEF HDYLGLCKYR 300
DCKHDTDPGC AIREAVEEGK IAETRFENYH RILESMAQVK TRKNFSDTDD 350 
Gene Ontology
 GO:0019003; F:GDP binding; IDA:EcoCyc.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042274; P:ribosomal small subunit biogenesis; IGI:EcoCyc. 
Interpro
 IPR010914; EngC_GTPase.
 IPR027417; P-loop_NTPase.
 IPR004881; Ribosome_biogen_GTPase_RsgA. 
Pfam
 PF03193; DUF258 
SMART
  
PROSITE
 PS50936; ENGC_GTPASE 
PRINTS