ID B1RAR5_CLOPF Unreviewed; 696 AA. AC B1RAR5; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 22-FEB-2023, entry version 66. DE RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872}; GN Name=fusA {ECO:0000313|EMBL:EDT22663.1}; GN ORFNames=AC1_0098 {ECO:0000313|EMBL:EDT22663.1}; OS Clostridium perfringens B str. ATCC 3626. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=451754 {ECO:0000313|EMBL:EDT22663.1, ECO:0000313|Proteomes:UP000004342}; RN [1] {ECO:0000313|EMBL:EDT22663.1, ECO:0000313|Proteomes:UP000004342} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B str. ATCC 3626 {ECO:0000313|Proteomes:UP000004342}; RA Paulsen I., Sebastian Y.; RT "Annotation of Clostridium perfringens B str. ATCC 3626."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000256|ARBA:ARBA00005870}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EDT22663.1}. 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 EMBL; ABDV01000030; EDT22663.1; -; Genomic_DNA. DR RefSeq; WP_003459930.1; NZ_ABDV01000030.1. DR AlphaFoldDB; B1RAR5; -. DR EnsemblBacteria; EDT22663; EDT22663; AC1_0098. DR Proteomes; UP000004342; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR CDD; cd04170; EF-G_bact; 1. DR CDD; cd16262; EFG_III; 1. DR CDD; cd01434; EFG_mtEFG1_IV; 1. DR CDD; cd03713; EFG_mtEFG_C; 1. DR CDD; cd04088; EFG_mtEFG_II; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR041095; EFG_II. DR InterPro; IPR009022; EFG_III. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR035649; EFG_V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR004540; Transl_elong_EFG/EF2. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR PANTHER; PTHR43261:SF6; ELONGATION FACTOR G-LIKE PROTEIN; 1. DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_III; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR TIGRFAMs; TIGR00484; EF-G; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Elongation factor {ECO:0000313|EMBL:EDT22663.1}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000313|EMBL:EDT22663.1}. FT DOMAIN 7..280 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT REGION 483..503 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 696 AA; 77249 MW; 4DCD2C0FF59E6A7D CRC64; MKEHKIENLR NIGIIGHSDS GKTALSEALL YYTKTTDRLG TCEDGNTISD YDQEEKKRKI SLALSIIPFE YDGTKINILD TPGYFDFVGE QIEGVKAADS AIITVCGVTG VQVGTEKAWE CCEKEKLPRA FFINKLDREN SNFDKVLENI RNIFGNKVIP TQYPLGKEKE FKGIVNLITE EAFEYDKKSG KINKIEIPNE VKDKVNEYRT YLMESVAETD EELLDKYLSE GELTVDEIYK GLSIGFEEGD IAPVMCGSSV SIVGMKSLLD SIKGYFPSPD ISKAKVAIDS NNKEILVKSN KDMPFSAFVF KTIADPFVGK LSIFKVQTGE LTTDKIIINS KNNKVEKVSS LCFLRGKSQI QTNKIGAGDI GAVTKLQYTS TGDTLCESNF KIAYEGFEFP EAVMTMAVLP KSKGDEEKIS QGLSKLLDED PTFKVSRDQE NAETLVSGIG ETHIEVLASK LKSKFGIDVI LKDPKIPYRE TIKGSSDVQG KHKKQSGGHG QYGDVKIKFE PRRDGELDLE FVDKVVGGVV PRNYIPAVEK GLRDCLKKGV LAGYPVIGIK ATLHDGSYHP VDSSEMAFKV AASLAYKKGM ENAKPVILEP IMKVEIIIPD EYMGDIISDI NKKRGRVIGM EPEGNNEKVI ADIPLSEMFK YATDLRSMTQ GRGSFSMEFE KYEEVPSTEV DKIIEDAKKM KEAKEA //