ID   IF2_CLOBB               Reviewed;         687 AA.
AC   B2TJ55;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CLL_A1273;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD22023.1; -; Genomic_DNA.
DR   RefSeq; WP_012422908.1; NC_018648.1.
DR   AlphaFoldDB; B2TJ55; -.
DR   SMR; B2TJ55; -.
DR   PRIDE; B2TJ55; -.
DR   EnsemblBacteria; ACD22023; ACD22023; CLL_A1273.
DR   KEGG; cbk:CLL_A1273; -.
DR   PATRIC; fig|935198.13.peg.1219; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001195; 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; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
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..687
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093774"
FT   DOMAIN          186..355
FT                   /note="tr-type G"
FT   REGION          195..202
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          220..224
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          241..244
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          295..298
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          331..333
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..202
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         241..245
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         295..298
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   687 AA;  75783 MW;  FD1B4A7CE6AED15D CRC64;
     MSKIRVYELA KELNVSSKDL ITLLMDEFGV EVKNHMSTIE DEEAQLIKEL LATKPEYIEG
     SLEDSKSLVD EYEEILQNEL NKAKKKRKKN KREDKDDENE ELETEVIEIG ETITVKELAE
     KLNKPSNDVI RTLIFSGVMA AINQEIDFAT AEKVCESYGV ILEKLEVTEE LEAVEAEDDD
     EENLTKRPPI VTVMGHVDHG KTSLLDAIRK AKVTDTEAGG ITQHIGAYTI NINGEEITFL
     DTPGHEAFTA MRARGAQVTD VVILVVAADD GIMPQTKEAI NHCKAAGVPM VVAINKIDKP
     GANPDRVKQE LTEHGLVVEE WGGDTICEEV SAKSNLNIEK LLEMVLLTAE MLELKANKER
     KAKGTVIEAK LDKGRGSVAT LLVQNGTLHV GDAIIVGSTY GRIRAMFDDT GKKIKSAGPS
     IPVEVLGLSE VPEAGDRFNQ VKDEKTARIM ADKRKDKEKS DSLMSGNRVS LEDLYSQIKE
     GKVKELGIIV KADVQGSVQA INQSLEKLST DDVKVRVIHS GVGAITETDI TLATASNAIV
     IGFNVRPDNN AVAQADKENV EIKTYRIIYD AIEDVKSAMI GMLEPEYKEV ILGSAEVRET
     YKISNVGTIA GCYVLNGKLQ RNAETRVIRD GIVIFESNLS SLKRFKDDVK EVNTGYECGL
     TVEKFNDVKE GDILECFMME AIKRKEL