ID   IF2_BACCQ               Reviewed;         686 AA.
AC   B9IVA1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-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=BCQ_3597;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM14025.1; -; Genomic_DNA.
DR   RefSeq; WP_000036342.1; NC_011969.1.
DR   AlphaFoldDB; B9IVA1; -.
DR   SMR; B9IVA1; -.
DR   EnsemblBacteria; ACM14025; ACM14025; BCQ_3597.
DR   GeneID; 64199152; -.
DR   KEGG; bcq:BCQ_3597; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000441; 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..686
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000118749"
FT   DOMAIN          188..357
FT                   /note="tr-type G"
FT   REGION          54..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..204
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          222..226
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          243..246
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          297..300
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          333..335
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        54..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         197..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         243..247
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         297..300
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   686 AA;  75726 MW;  E981BBB3FA1A9A00 CRC64;
     MSKIRVHEYA KKHNISSKDL MTKLKEMNIE VSNHMTMLDD EVVNKLDNEY QAEKPSVADE
     FEVEEKVVRS KKNSNKKKKK GKGNEDKRQE NFAGRQQTQT VETPDKITFS GSLTVGDLAK
     KLSKEPSEII KKLFMLGIMA TINQDLDKDT IELIANDYGI EVEEEVIVSE TEFETFIDEQ
     DDEENLKERP AVVTIMGHVD HGKTTLLDSI RNSKVTAGEA GGITQHIGAY QVEVNDKKIT
     FLDTPGHAAF TTMRARGAQV TDITILVVAA DDGVMPQTVE AINHAKAAGV PIIVAVNKMD
     KPAANPDRVM QELTEYELVP EAWGGDTIFV PISAIQGEGI DNLLEMILLV SEVEEYKANP
     NRYATGTVIE AQLDKGKGTI ATLLVQNGTL RVGDPIVVGT TFGRVRAMVS DIGRRVKVAG
     PSTPVEITGL NEVPQAGDRF MAFADEKKAR QIGESRAQEA LLAQRGEKSK LSLEDLFQQI
     QEGDVKEINL IVKADVQGSV EAMAASLRKI DVEGVKVKII HTGVGAITES DIILASASNA
     IVIGFNVRPD VNAKRTAELE NVDIRLHRII YKVIEEIEAA MQGMLDPEFE EKVIGQAEVR
     QTFKVTKVGT IAGCYVTDGK ITRDSGVRII RDGVVIYEGQ LDTLKRFKDD VKEVAQNYEC
     GITIEKYNDL KEGDIIEAYI MEEVKR