ID   IF2_KOSOT               Reviewed;         695 AA.
AC   C5CDZ4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Kole_1403;
OS   Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC   Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga.
OX   NCBI_TaxID=521045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Noll K.;
RT   "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL   Submitted (JUN-2009) 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; CP001634; ACR80096.1; -; Genomic_DNA.
DR   RefSeq; WP_015868743.1; NC_012785.1.
DR   AlphaFoldDB; C5CDZ4; -.
DR   SMR; C5CDZ4; -.
DR   STRING; 521045.Kole_1403; -.
DR   PRIDE; C5CDZ4; -.
DR   EnsemblBacteria; ACR80096; ACR80096; Kole_1403.
DR   KEGG; kol:Kole_1403; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002382; 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; 1.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..695
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000202778"
FT   DOMAIN          184..358
FT                   /note="tr-type G"
FT   REGION          60..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..200
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          218..222
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          239..242
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          293..296
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          330..332
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..200
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         239..243
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         293..296
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   695 AA;  77427 MW;  1535E99643DB5EB8 CRC64;
     MAKTRVYELA KRLKITTREL IDELEELGVS VKSHMSVLDD EIVNIIVGLY EEEEKAAKIK
     KSASSKKKTE KEVEEEEIET PKKKKKQEEK IPGEEKVLRI TPDELKLDLL AEKMRVPVSK
     IVKDHFMKGI ILRPAQSLSL EDANQIAAQY GWKLEIEKEE MADPLEALKK KYEELYKDES
     RLVQRPPVVT VMGHVDHGKT TLLDRIRKTS IAEKEVGGIT QSIGAYHVEV NGKKITFIDT
     PGHEAFTEMR ARGAQATDIV ILVVAADDGV MPQTVEAYNH AKTAQVPIIV AINKIDKPNA
     SIEATKQQLA SKLGLVPEDW GGDTIVVPIS AKTGQGIDEL LEMILLVAEM SEIKCIPTGN
     ARGIIIESEL DKGVGPLATV IVKDGILEAG DYIVAGATYG KVRALRDEKG KRVKKAVPGD
     PVQIIGFNEV PDVHAILYVV DSLDQAREVA AFAQEKQKKE KLLKGKRHVR LEEFMRIGGK
     DETKVLNLIL KSDSFGSVEA LRQTIAKLET EEVHIEVVHF GIGTINASDV MLAAASDAVI
     IGYKVKPDSQ ARRQAEEEGV QIRVYQVIFD LIDDLKKALE GLLEPEEIDE TVGHGEIRKV
     FKIKKVGSIA GVQLLDGYVT KKGFVRIYRN NQEIFDGEIE SLKHYKDEVS RIDAPKECGI
     KFLNFDDIQE GDQLEFHVKR KVKRTLDFNE SSSDS