ID   IF2_THEP1               Reviewed;         693 AA.
AC   A5IJ09;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tpet_0153;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) 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; CP000702; ABQ46182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5IJ09; -.
DR   SMR; A5IJ09; -.
DR   STRING; 390874.Tpet_0153; -.
DR   EnsemblBacteria; ABQ46182; ABQ46182; Tpet_0153.
DR   KEGG; tpt:Tpet_0153; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000006558; 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..693
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335517"
FT   DOMAIN          181..349
FT                   /note="tr-type G"
FT   REGION          190..197
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          215..219
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          236..239
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          290..293
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          327..329
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..197
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         236..240
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         290..293
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   693 AA;  78265 MW;  9FEF9245988501EC CRC64;
     MIEMARLRVY ELARKLNMSP KELLQELEEL GVNVKSHMSY VDEEMANIII DLLEEDNRKA
     KQPSKPKKEK GEEEVEKEVV EKKKKKKITL KPDELKLDII AEKIGVPQNK IIQDMFVKRG
     IALRPGQILK LEEVEQILKE YKIEIEIEEE QQTSVEEVDE FELLEKRYQE LYEKEKDKLV
     PRPPVVTVMG HVDHGKTTLL DRIRSTRVAE REEGGITQSI GAYQVEVNGK KITFIDTPGH
     ELFTEMRARG AQATDIVVLV VAADDGVMPQ TIEAYNHAKA ANVPIIVAIN KIDKPNANVE
     KTKQELVEKL GLIPEEWGGD TIVVPISART GQGVDELLEM ILLVAEMNEI KCYPEGPARA
     VIIESKLDKK MGPVASVIVK DGVLKVGDAV VASNTYGRVR NLFDDNMRPI REAYPSQPVM
     ILGFEDVPDV HSNVYVVESA EKAKEIVEKR LQRLEAQKQS RKHINLEELM KMMQEKEKKV
     LNLILKADTY GSVAALKNAI NKLQSKEIEL NIVHAGVGEI STSDVMLAAA VDGVILGFRV
     KVNNQARRLA EQEGVDVRTY SIIYKLVEDL KLALEGMLEP EEVEEVIGHG EIRKVFKISK
     VGKVAGVQML DGKADRNGFV RIYRNGQLVF EGKIESLKHY KEDVNVVEAP QECGIKFAGF
     DDIQEGDELE FYVIRKVKRK PTFVEEQADQ EQK