ID   IF2_THESQ               Reviewed;         690 AA.
AC   B1L7T1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, 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=TRQ2_0151;
OS   Thermotoga sp. (strain RQ2).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC   unclassified Thermotoga.
OX   NCBI_TaxID=126740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RQ2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga sp. RQ2.";
RL   Submitted (MAR-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; CP000969; ACB08512.1; -; Genomic_DNA.
DR   RefSeq; WP_012310348.1; NC_010483.1.
DR   AlphaFoldDB; B1L7T1; -.
DR   SMR; B1L7T1; -.
DR   PRIDE; B1L7T1; -.
DR   EnsemblBacteria; ACB08512; ACB08512; TRQ2_0151.
DR   KEGG; trq:TRQ2_0151; -.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001687; 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.
FT   CHAIN           1..690
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093840"
FT   DOMAIN          178..346
FT                   /note="tr-type G"
FT   REGION          187..194
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          212..216
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          233..236
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          287..290
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          324..326
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         233..237
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         287..290
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   690 AA;  77894 MW;  14925D1B95E7B6FA CRC64;
     MARLRVYELA RKLNMSPKEL LQELEELGVN VKSHMSYVDE EMANIIIDLL EEDNRKAKQP
     SKPKKEKGEE EVEKEVVEKK KKKKITLKPD ELKLDIIAEK IGVPQNKIIQ DMFVKRGIAL
     RPGQILKLEE VEQILKEYKI EIEIEEEQQT SVEEVDEFEL LEKRYQELYE KEKDKLVPRP
     PVVTVMGHVD HGKTTLLDRI RSTRVAEREE GGITQSIGAY QVEVNGKKIT FIDTPGHELF
     TEMRARGAQA TDIVVLVVAA DDGVMPQTIE AYNHAKAANV PIIVAINKID KPNANVEKTK
     QELVEKLGLI PEEWGGDTIV VPISARTGQG VDELLEMILL VAEMNEIKCY PEGPARAVII
     ESKLDKKMGP VASVIVKDGV LKVGDAVVAS NTYGKVRNLF DDNMRPIREA YPSQPVMILG
     FEDVPDVHSN VYVVESVEKA KEIVEKRLQR LEAQKQSRKH INLEDLMKMM QEKEKKVLNL
     ILKADTYGSV AALKNAINKL QSKEIELNIV HAGVGEISTS DVMLAAAVDG VILGFRVKVN
     NQARRLAEQE GVDVRTYSII YKLVEDLKLA LEGMLEPEEV EEVIGHGEIR KVFKISKVGK
     VAGVQMLDGK ADRNGFVRIY RNGQLVFEGK IESLKHYKED VNVVEAPQEC GIKFAGFDDI
     QEGDELEFYV IRKVKRKPTF VEEQSDQEQK