ID IF2_BACCQ Reviewed; 686 AA. AC B9IVA1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 14-DEC-2022, entry version 76. DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100}; GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BCQ_3597; OS Bacillus cereus (strain Q1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=361100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q1; RX PubMed=19060151; DOI=10.1128/jb.01629-08; RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., RA Xue Y., Zhu Y., Jin Q.; RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1 RT with industrial applications."; RL J. Bacteriol. 191:1120-1121(2009). 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; CP000227; ACM14025.1; -; Genomic_DNA. DR RefSeq; WP_000036342.1; NC_011969.1. DR AlphaFoldDB; B9IVA1; -. DR SMR; B9IVA1; -. DR EnsemblBacteria; ACM14025; ACM14025; BCQ_3597. DR GeneID; 64199152; -. DR KEGG; bcq:BCQ_3597; -. DR HOGENOM; CLU_006301_5_1_9; -. DR OMA; NRDNRTG; -. DR Proteomes; UP000000441; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule. DR CDD; cd03702; IF2_mtIF2_II; 1. DR Gene3D; 3.40.50.10050; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00100_B; IF_2_B; 1. DR InterPro; IPR044145; IF2_II. DR InterPro; IPR006847; IF2_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. 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 PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF11987; IF-2; 1. DR Pfam; PF04760; IF2_N; 2. DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 2. DR TIGRFAMs; TIGR00487; IF-2; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. 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..686 FT /note="Translation initiation factor IF-2" FT /id="PRO_1000118749" FT DOMAIN 188..357 FT /note="tr-type G" FT REGION 54..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 197..204 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 222..226 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 243..246 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 297..300 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 333..335 FT /note="G5" FT /evidence="ECO:0000250" FT COMPBIAS 54..71 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 197..204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 243..247 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 297..300 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" SQ SEQUENCE 686 AA; 75726 MW; E981BBB3FA1A9A00 CRC64; MSKIRVHEYA KKHNISSKDL MTKLKEMNIE VSNHMTMLDD EVVNKLDNEY QAEKPSVADE FEVEEKVVRS KKNSNKKKKK GKGNEDKRQE NFAGRQQTQT VETPDKITFS GSLTVGDLAK KLSKEPSEII KKLFMLGIMA TINQDLDKDT IELIANDYGI EVEEEVIVSE TEFETFIDEQ DDEENLKERP AVVTIMGHVD HGKTTLLDSI RNSKVTAGEA GGITQHIGAY QVEVNDKKIT FLDTPGHAAF TTMRARGAQV TDITILVVAA DDGVMPQTVE AINHAKAAGV PIIVAVNKMD KPAANPDRVM QELTEYELVP EAWGGDTIFV PISAIQGEGI DNLLEMILLV SEVEEYKANP NRYATGTVIE AQLDKGKGTI ATLLVQNGTL RVGDPIVVGT TFGRVRAMVS DIGRRVKVAG PSTPVEITGL NEVPQAGDRF MAFADEKKAR QIGESRAQEA LLAQRGEKSK LSLEDLFQQI QEGDVKEINL IVKADVQGSV EAMAASLRKI DVEGVKVKII HTGVGAITES DIILASASNA IVIGFNVRPD VNAKRTAELE NVDIRLHRII YKVIEEIEAA MQGMLDPEFE EKVIGQAEVR QTFKVTKVGT IAGCYVTDGK ITRDSGVRII RDGVVIYEGQ LDTLKRFKDD VKEVAQNYEC GITIEKYNDL KEGDIIEAYI MEEVKR //