ID   IF2_CLOBA               Reviewed;         687 AA.
AC   B2V4G9;
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=CLH_1224;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
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 genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-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; CP001078; ACD52052.1; -; Genomic_DNA.
DR   RefSeq; WP_003370394.1; NC_010723.1.
DR   AlphaFoldDB; B2V4G9; -.
DR   SMR; B2V4G9; -.
DR   KEGG; cbt:CLH_1224; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
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_1000093773"
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;  75774 MW;  421725109A68906D CRC64;
     MSKIRVYELA KELNVSSKDL ITLLMDEFGV EVKNHMSAIE DEEAQLIKEL LATKPEYVEG
     SLEDSKSLVD EYEEILQNEL NKAKKKRKKN KREDKDDENE ELETEVIEIG ETITVKELAE
     KLNKPSNDVI RTLIFSGVMA AINQEIDFAT AEKVCESYGV ILEKLEVIEE LEAVEVEEDD
     EENLEKRPPI VTVMGHVDHG KTSLLDAIRK AKVTDTEAGG ITQHIGAYTI NINGEEITFL
     DTPGHEAFTA MRARGAQVTD VVILVVAADD GIMPQTKEAI NHCKAAGVPM VVAINKIDKP
     GANPDRVKQE LTEHGLVVEE WGGDTICEEV SAKSNLNIEK LLEMVLLTAE MLELKANKER
     KAKGTVIEAK LDKGRGPVAT LLVQNGTLHV GDAIIVGSTY GRIRAMFDDT GKKIKSAGPS
     IPVEVLGLSE VPEAGDRFNQ VKDEKTARIM ADKRKDKEKS DSLMSGNRVS LEDLYSQIKE
     GKVKELGIIV KADVQGSVQA INQSLEKLST DDVKVRVIHG GVGAITETDI TLATASNAIV
     IGFNVRPDNN AVAQADKENV EIKTYRIIYD AIEDVKSAMI GMLEPEYKEV ILGSAEVRET
     YKISNVGTIA GCYVLNGKLQ RNAETRVIRD GIVIFESSLS SLKRFKDDVK EVNTGYECGL
     TVEKFNDVKE GDILECFMME AIKRKEL