ID   IF2_CLOBJ               Reviewed;         688 AA.
AC   C1FS59;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CLM_2711;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-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; CP001581; ACO84307.1; -; Genomic_DNA.
DR   RefSeq; WP_012704158.1; NC_012563.1.
DR   AlphaFoldDB; C1FS59; -.
DR   SMR; C1FS59; -.
DR   STRING; 536232.CLM_2711; -.
DR   EnsemblBacteria; ACO84307; ACO84307; CLM_2711.
DR   KEGG; cby:CLM_2711; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001374; 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..688
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000118755"
FT   DOMAIN          187..354
FT                   /note="tr-type G"
FT   REGION          53..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..203
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          221..225
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          242..245
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          296..299
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          332..334
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        53..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         196..203
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         242..246
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         296..299
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   688 AA;  75824 MW;  E457067D6444BD9F CRC64;
     MAKIRVYELA KELNISSKEL ITLLEEEFSV EVKNHMSAIE DEDANLIKEL LSGKEKSEKT
     KEEDDEIETT AKNPIKESMN NKKSNKRDDK NEKVNTENAE DMGIITMTSD TITVKEISDK
     LEKSYAEVIK ELMLMGVMAS VNQEINFEMA EKLAAKFDME ILKEDEDEKE DLEDILKDNE
     EEEYLQKRSP IITVMGHVDH GKTSLLDAIR KSKITSTEAG GITQHIGAYT VELNGEAITF
     LDTPGHAAFT AMRARGAQVT DIVILVVAAD DGIMPQTQEA ISHCKAANVP LIVAINKIDR
     PGANIDKVKQ ELTEYGLVAE DWGGDTICVP VSAHTKEGID DLLEMILLSS EILELKANPN
     RKAKGTVVEA KLDKGRGPVA TLLIQNGTLR VGDSIVVGST YGRIRAMFND KGRNIESAGP
     STPVEILGLS EVPEAGDKFY QVKEEKTARG IADKRKEKIR DEYLQSTHKV SLEDLYNQIQ
     EGTVKELGLI VKADVQGSVE ALKQSLEKLS TEEVKVRVIH GGVGAINETD VTLATASNGI
     ILGFNVRPDN NAIIASERDG VDIKTYRVIY DAIEDIKSAM LGMLEPEFKE VVIGTAEVRQ
     VYKISSVGTI AGAYIQTGKL ARNAGARVIR DGIVIFESEL ASLKRFKDDA KEVAQGYECG
     LSIEKFNDIK EGDIIECFIM EEIKKKTL