ID EFG_CLOPA Reviewed; 11 AA. AC P81350; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 03-APR-2013, entry version 33. DE RecName: Full=Elongation factor G; DE Short=EF-G; DE AltName: Full=CP 5; DE Flags: Fragment; GN Name=fusA; OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5; RX PubMed=9629918; DOI=10.1002/elps.1150190533; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step CC during translation elongation. During this step, the ribosome CC changes from the pre-translocational (PRE) to the post- CC translocational (POST) state as the newly formed A-site-bound CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E CC sites, respectively. Catalyzes the coordinated movement of the two CC tRNA molecules, the mRNA and conformational changes in the CC ribosome (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. CC EF-G/EF-2 subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR PROSITE; PS00301; EFACTOR_GTP; PARTIAL. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 >11 Elongation factor G. FT /FTId=PRO_0000091108. FT NON_TER 11 11 SQ SEQUENCE 11 AA; 1337 MW; 412E71F1D9C33B17 CRC64; KYPLEKFQNI G //