ID   IF2_CLOBL               Reviewed;         688 AA.
AC   A7GG06;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CLI_2474;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) 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; CP000728; ABS40489.1; -; Genomic_DNA.
DR   RefSeq; WP_012100373.1; NC_009699.1.
DR   AlphaFoldDB; A7GG06; -.
DR   SMR; A7GG06; -.
DR   EnsemblBacteria; ABS40489; ABS40489; CLI_2474.
DR   KEGG; cbf:CLI_2474; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002410; 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_1000008231"
FT   DOMAIN          187..354
FT                   /note="tr-type G"
FT   REGION          50..95
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        50..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..95
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;  75590 MW;  2333374905873860 CRC64;
     MAKIRVYELA KELNISSKEL ITLLEEEFSV EVKNHMSAIE DEDADLIKEL LSGKEKSEKT
     KEEDDEIETT AKNPIKESIN NKKSNKRDDK NEKVNTENAE DMAIITMTSD TITVKEISDK
     LEKSYAEVIK ELMLMGVMAS VNQEINFEMA EKLAAKFDTE ILKEEQDEED DLEDILKDSE
     EEENLQKRSP IITVMGHVDH GKTSLLDAIR KSKVTSTEAG GITQHIGAYT VELNGESITF
     LDTPGHAAFT AMRARGAQVT DIVILVVAAD DGIMPQTKEA ISHCKAAEVP LIVAINKIDR
     PGANIDKVKQ ELTEYGLVAE DWGGDTVCVP VSAHTKEGID ELLEMILLSS EILELKANPN
     RKAKGTVVEA KLDKGRGPVA TLLVQNGTLT VGDSIVVGST YGRIRAMFND KGENIQSAGP
     STPVGILGLS EVPEAGDKFY QVKDEKTARG IADKRKEKIR DEYLQSTHKV SLEDLYNQIR
     EGKVKELGLI VKADVQGSVE ALKQSLEKLS TEEVKVRVIH GGVGAINETD VTLATASNGI
     ILGFNVRPDN NAIIASERDG VDIKTYRVIY DAIEDIKSAM LGMLEPEFKE VVIGTAEVRQ
     VYKISSVGTI AGAYVQTGKL ARNAGARVIR DGIVIFESEL ASLKRFKDDA KEVAQGYECG
     LSIEKFNDIK EGDIIECFIM EEIKKKTL