ID IF2_FRATW Reviewed; 843 AA. AC A4IW10; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 1. DT 29-SEP-2021, entry version 86. DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100}; GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=FTW_0126; OS Francisella tularensis subsp. tularensis (strain WY96-3418). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=418136; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WY96-3418; RX PubMed=17895988; DOI=10.1371/journal.pone.0000947; RA Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V., RA Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D., RA Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J., RA Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.; RT "Complete genomic characterization of a pathogenic A.II strain of RT Francisella tularensis subspecies tularensis."; RL PLoS ONE 2:E947-E947(2007). 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; CP000608; ABO46112.1; -; Genomic_DNA. DR RefSeq; WP_003024583.1; NC_009257.1. DR SMR; A4IW10; -. DR KEGG; ftw:FTW_0126; -. DR HOGENOM; CLU_006301_6_2_6; -. DR OMA; NRDNRTG; -. DR BioCyc; FTUL418136:G1G8F-122-MONOMER; -. 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; IPR009061; DNA-bd_dom_put_sf. 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; PTHR43381; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF11987; IF-2; 1. DR Pfam; PF04760; IF2_N; 2. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50447; SSF50447; 2. DR SUPFAM; SSF52156; SSF52156; 1. DR SUPFAM; SSF52540; SSF52540; 1. 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..843 FT /note="Translation initiation factor IF-2" FT /id="PRO_1000008247" FT DOMAIN 345..512 FT /note="tr-type G" FT NP_BIND 354..361 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT NP_BIND 400..404 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT NP_BIND 454..457 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT REGION 198..219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 354..361 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 379..383 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 400..403 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 454..457 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 490..492 FT /note="G5" FT /evidence="ECO:0000250" SQ SEQUENCE 843 AA; 92033 MW; D88627DBE77A16F3 CRC64; MAEITVGQLA QQTNKEVDAL LKQLKSFGIE KSSEKDTLTP TEMKTLLEKI NSAKNTATRK KVTSVKLDGK HKINVSVKRK RRVAKKVEQQ ESTTLEQPQE LETMVQEVSQ QVDIVKEQDN IEQIVENKEA VKVQEQRQAE IAKPVIKDSG FKITAMPEIK IEEIVAEDDE GLAASDKQAK KKAAKKVFSE AVNTNTKYKR EEEEKKSKAK KAGGKGFKKA NPRQLSQLAG DLESFDEFGA KKGKLKAPKV KKQEFTKPVE NTVRTVEIHE GITVSELAQK MAVKGAEIVK VLFNMGVMAT INQSLDQDTA ILIVEEMGHK YTLHNENALE EAVTIVDRSS YKKISRAPVV TIMGHVDHGK TSLLDYIRQT RVVAGEAGGI TQHIGAYSVK TDKGSITFLD TPGHEAFTSM RARGAKSTDI VILVVAADDG VMPQTEEAIQ HAKAARVPIV VAVNKIDKPE ADPDKVISEL AQRNVIPESW GGDVMFVNVS AKTGEGVADL LEAVLLQSEV LELEAFAEGL AEGVVIESRL EKGRGPVATV LVQNGNLKQG DNILCGTEYG RVRAMHNDLG KKIKAAGPAT PVEILGLSGV PAAGDEMVVI ENEKKAKELA AQRSQKQKEA KIAQEQSLKL SNMFNNMGKE GEQQVLKIIL KGDVQGSVEA IRESLLKLST DEVKVDIIAS GIGAITSSDV TLAVASTAVV IGFNVRADSA AKKLAETDGV EFRYYNIIYD LIDDVKKAMS GLLSPEMKEQ IIGIAEVREV YRSSKFGSIA GCMVIEGVVK RTNPIRVLRN NVVIYEGTLE SLKRFKDDAS EVKKGLECGI GVKNYNDVRE GDQIEVFEVA KEL //