ID   IF2_FRATM               Reviewed;         846 AA.
AC   B2SEW7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=FTM_0114;
OS   Francisella tularensis subsp. mediasiatica (strain FSC147).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=441952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC147;
RX   PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA   Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA   Keim P., Johansson A.;
RT   "Molecular evolutionary consequences of niche restriction in Francisella
RT   tularensis, a facultative intracellular pathogen.";
RL   PLoS Pathog. 5:E1000472-E1000472(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}.
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DR   EMBL; CP000915; ACD30212.1; -; Genomic_DNA.
DR   RefSeq; WP_012429080.1; NC_010677.1.
DR   AlphaFoldDB; B2SEW7; -.
DR   SMR; B2SEW7; -.
DR   KEGG; ftm:FTM_0114; -.
DR   HOGENOM; CLU_006301_6_2_6; -.
DR   OMA; NRDNRTG; -.
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..846
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093787"
FT   DOMAIN          345..512
FT                   /note="tr-type G"
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"
FT   BINDING         354..361
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         400..404
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         454..457
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   846 AA;  92374 MW;  28D528526FFFF667 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 GDQIEVFEVI
     EVAKEL