ID IF2_ACIBS Reviewed; 899 AA. AC B0VLU2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 105. DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100}; GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; GN OrderedLocusNames=ABSDF3180; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- FUNCTION: One of the essential components for the initiation of protein CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis CC and promotes its binding to the 30S ribosomal subunits. Also involved CC in the hydrolysis of GTP during the formation of the 70S ribosomal CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. IF-2 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00100}. 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; CU468230; CAP02458.1; -; Genomic_DNA. DR AlphaFoldDB; B0VLU2; -. DR SMR; B0VLU2; -. DR KEGG; abm:ABSDF3180; -. DR HOGENOM; CLU_006301_6_2_6; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule. DR CDD; cd01887; IF2_eIF5B; 1. DR CDD; cd03702; IF2_mtIF2_II; 1. DR CDD; cd03692; mtIF2_IVc; 1. DR FunFam; 2.40.30.10:FF:000007; Translation initiation factor IF-2; 1. DR FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1. DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1. DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1. DR HAMAP; MF_00100_B; IF_2_B; 1. DR InterPro; IPR009061; DNA-bd_dom_put_sf. DR InterPro; IPR053905; EF-G-like_DII. DR InterPro; IPR013575; IF2_assoc_dom_bac. DR InterPro; IPR044145; IF2_II. DR InterPro; IPR006847; IF2_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR000178; TF_IF2_bacterial-like. DR InterPro; IPR015760; TIF_IF2. DR InterPro; IPR023115; TIF_IF2_dom3. DR InterPro; IPR036925; TIF_IF2_dom3_sf. DR InterPro; IPR009000; Transl_B-barrel_sf. DR NCBIfam; TIGR00487; IF-2; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1. DR Pfam; PF22042; EF-G_D2; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF11987; IF-2; 1. DR Pfam; PF08364; IF2_assoc; 1. DR Pfam; PF04760; IF2_N; 1. DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF46955; Putative DNA-binding domain; 1. DR SUPFAM; SSF50447; Translation proteins; 2. DR PROSITE; PS51722; G_TR_2; 1. DR PROSITE; PS01176; IF2; 1. PE 3: Inferred from homology; KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding; KW Protein biosynthesis. FT CHAIN 1..899 FT /note="Translation initiation factor IF-2" FT /id="PRO_1000093750" FT DOMAIN 399..568 FT /note="tr-type G" FT REGION 115..137 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..189 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 262..309 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 408..415 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 433..437 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 454..457 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 508..511 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 544..546 FT /note="G5" FT /evidence="ECO:0000250" FT BINDING 408..415 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 454..458 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 508..511 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" SQ SEQUENCE 899 AA; 97297 MW; 832E70ED099C9BFD CRC64; MTDKSIKELA LSVGRPVEKL LEQAREAGLP QRTADDIITT EQQDTLVNYL KKVHGQESGN TGKIALKRKT TSTAKVASTS GKAKTINVEV RKKQVFAKPN PEQIAAEAKA RAEAEAKARA EQQAREAAEQ KARLQTEQKA KATLDAMRAA HQQDSAAQSA PKAAVVVEKR GGGTVKPAPK PAETLEQKKA REAQTAQLKA TEEAARRKAA EEAQQRTLEQ MRKMASKYSN DDATATIRVI DDSPLASGLV GQAYEDSFNQ EDREIKRGGA TTNPRAGKKG GRRGQEEQSF VNHNKRGLKS SQANKHGFEK PVKKQVYDVE IGSSIVVADL AQKMAIKVRE VIKTLMKMGE LVNQNQTIDQ DTAALVVEEM GHNPVLVSDT QAEDNLLEAA EEARGEQTTR PPVVTIMGHV DHGKTSLLDR IRRSKVAAGE AGGITQHIGA YHVETDKGII TFLDTPGHAA FTSMRARGAK ATDIVVLVVA ADDGVMPQTA EAIDHARAAG TPIIVAINKM DKESADPDRV LNELTTKEIV PEEWGGDVPV AKVSAHTGQG IDELLDLILI QSELMELKAS AEGAAQGVVI EARVDKGRGA VTSILVQNGT LNIGDLVLAG SSYGRVRAMS DENGKPIKSA GPSIPVEILG LPEAPMAGDE VLVVNDEKKA REVADARADR EREKRIERQS AMRLENIMAS MGKKDVPTVN VVLRTDVRGT LEALNAALHE LSTDEVKVRV ISSGVGAITE SDVILAESSE AVLLGFNVRA DTAARQKSDQ DGIDIRYYSI IYELIDDVKD AMSGKLAPEH RETILGVAQV REVFRSSKFG AAAGCMVMEG VIHRNKPIRV LRDDVVIFQG ELESLRRYKD VVDEVRAGME CGLAVKGYND IKPLDKIEVY DVQIVKRSL //