ID   IF2_BACC2               Reviewed;         688 AA.
AC   B7IUH1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-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};
GN   OrderedLocusNames=BCG9842_B1333;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
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; CP001186; ACK96313.1; -; Genomic_DNA.
DR   RefSeq; WP_000036346.1; NC_011772.1.
DR   AlphaFoldDB; B7IUH1; -.
DR   SMR; B7IUH1; -.
DR   EnsemblBacteria; ACK96313; ACK96313; BCG9842_B1333.
DR   KEGG; bcg:BCG9842_B1333; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000006744; 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_1000117321"
FT   DOMAIN          190..359
FT                   /note="tr-type G"
FT   REGION          62..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..206
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          224..228
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          245..248
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          299..302
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          335..337
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         245..249
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         299..302
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   688 AA;  75906 MW;  0DCC6FFB180BBA68 CRC64;
     MSKIRVHEYA KKNNISSKDL MTKLKEMNIE VSNHMTMLED EVVNKLDNEY NTGAEKPSVA
     DEFEVEEKVV RSKKNSNKKK KKGKGNEDKR QDNFAGRQQT QIVETPDKIT FSGSLTVGEL
     AKKLSKEPSE IIKKLFMLGI MATINQDLDK DTIELIATDY GIEVEEEIVV SETEFETFMD
     EQDDEENLKE RPAVVTIMGH VDHGKTTLLD SIRNSKVTAG EAGGITQHIG AYQVEVNDKK
     ITFLDTPGHA AFTTMRARGA QVTDITILVV AADDGVMPQT VEAISHAKAA GVPIIVAVNK
     MDKPAANPDR VMQELTEYEL VPEAWGGDTI FVPISAIQGE GIDNLLEMIL LVSEVEEYKA
     NPNRYATGTV IEAQLDKGKG TIATLLVQNG TLRVGDPIVV GTSFGRVRAM VSDIGRRVKV
     AGPSTPVEIT GLNEVPQAGD RFMAFADEKK ARQIGESRAQ EALVAQRGEK SKLSLEDLFQ
     QIQESDVKEI NLIVKADVQG SVEAMAASLR KIDVEGVKVK IIHTGVGAIT ESDIILASAS
     NAIVIGFNVR PDVNAKRTAE LENVDVRLHR IIYKVIEEIE LAMQGMLDPE FEEKVIGQAE
     VRQTFKVTKV GTIAGCYVID GKITRDSGVR IIRDGIVIFE GQLDTLKRFK DDVKEVAQNY
     ECGITIERYN DLKEGDIIEA YVMEEVKR