ID   IF2_CLOB6               Reviewed;         688 AA.
AC   C3L0B6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-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=CLJ_B2643;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
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; CP001083; ACQ52939.1; -; Genomic_DNA.
DR   RefSeq; WP_003362559.1; NC_012658.1.
DR   AlphaFoldDB; C3L0B6; -.
DR   SMR; C3L0B6; -.
DR   EnsemblBacteria; ACQ52939; ACQ52939; CLJ_B2643.
DR   KEGG; cbi:CLJ_B2643; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002333; 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_1000202767"
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;  75727 MW;  506F58714FE08B07 CRC64;
     MAKIRVYELA KELNISSKEL ITLLEEEFSV EVKNHMSAIE DEDADLIKEL LSGKEKSEKT
     KEEDDEIETT AKNPIKESIN NKKSNKRDDK KEKVNTENAE DMGIITMTSD TITVKEISDK
     LEKSYAEVIK ELMLMGVMAS VNQEINFEMA EKLAAKFDME ILKEDEDEEE DLEDILKDNE
     EEEHLQKRSP IITVMGHVDH GKTSLLDAIR KSKVTSTEAG GITQHIGAYT VELNGEAITF
     LDTPGHAAFT AMRARGAQVT DIVILVVAAD DGIMPQTQEA ISHCKAANVP LIVAINKIDR
     PGANIDKVKQ ELTEYGLVAE DWGGDTICVP VSAHTKEGID DLLEMILLSS EILELKANPN
     RKAKGTVVEA KLDKGRGAVA TLLIQNGTLR VGDSIVVGST YGRIRAMFND KGRNIKSAGP
     STPVEILGLS EVPEAGDKFY QVKDEKTARG IADKRKEKIR DEYLQSTHKV SLEDLYNQIQ
     EGTVKELGLI VKADVQGSVE ALKQSLEKLS TEEVKVRVIH GGVGAINETD VTLATASNGI
     ILGFNVRPDN NAIIASERDG VDIKTYRVIY DAIEDIKSAM LGMLEPEFKE VVIGTAEVRQ
     VYKISSVGTI AGAYVQTGKL ARNAGARVIR DGIVIFESEL ASLKRFKDDA KEVAQGYECG
     LSIEKFNDIK EGDIIECFIM EEIKKKTL