ID   IF2_THEAB               Reviewed;         696 AA.
AC   B7IF03;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=THA_160;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(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; CP001185; ACJ74667.1; -; Genomic_DNA.
DR   RefSeq; WP_012579381.1; NC_011653.1.
DR   AlphaFoldDB; B7IF03; -.
DR   SMR; B7IF03; -.
DR   STRING; 484019.THA_160; -.
DR   EnsemblBacteria; ACJ74667; ACJ74667; THA_160.
DR   KEGG; taf:THA_160; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002453; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..696
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000117338"
FT   DOMAIN          187..361
FT                   /note="tr-type G"
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          333..335
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
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   696 AA;  78610 MW;  9E3E3DBDB8DF8DC4 CRC64;
     MARLRVYELA RQLEMDTREL MKELHELGIE IKSHMSYIDE ETVNLLLEMY GTQEEEEELI
     EEYEEYEEID EEVNGKHFKN KEGSLEKLQT NKKKNSVKIT EEDLKLDKFA EKIGIPQNKI
     IQDFFMKGEI LKPGQSLNLQ LAKKIAKMYD VRISFENEEK EEVIENPLIE IEKYFEEKYK
     NPENLKERPP VVTVMGHVDH GKTTLLDYIR NTRVAEREEG GITQSIGAYQ VEVNGKKITF
     IDTPGHEIFT EMRARGAQAT DIVVLVVAAD DGVMPQTIEA YNHAKSANVP IIVAINKIDK
     PNANVEKTKQ ELVNKLNLIP EEWGGDTIVV PISAKKGQNV DTLLEMILLV AEMQEIKGIP
     DGPVRAVTIE SKLDKGFGPV ANVIVKDGIL KIGDYIISGK VMGKVKALVN DQGKRVKEAG
     PSTPVMIVGF EELPDSHGIV YSVDSLDKAR EISEKIREIE QKELRRKRHM KLEEILKMME
     QSERKELRLV LKADTQGSLM ALSGAINKLR SEEISINIIH SGVGSITVSD VMLATASDAI
     ILGFRVKADS QARKMAEAEG IQIKTYTIVY KLIEELQAAL EGMLEPEEIE EITGRGEIKK
     VFKIKKVGSI AGVQMIEGYV EKDGLVKVYR SGKLVYEGKI ESLKHYQQDV KRVDAPQECG
     IKLENFDDIK EGDELEFSVL KKVARKLTFE EDKGEK