ID   IF2_THEPX               Reviewed;         692 AA.
AC   B0K1D6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=Teth514_1645;
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter;
OC   unclassified Thermoanaerobacter.
OX   NCBI_TaxID=399726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514;
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., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-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; CP000923; ABY92931.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0K1D6; -.
DR   SMR; B0K1D6; -.
DR   EnsemblBacteria; ABY92931; ABY92931; Teth514_1645.
DR   KEGG; tex:Teth514_1645; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002155; 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..692
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093839"
FT   DOMAIN          194..363
FT                   /note="tr-type G"
FT   REGION          203..210
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          228..232
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          249..252
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          303..306
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          339..341
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         203..210
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         249..253
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         303..306
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   692 AA;  77133 MW;  9D6561586503B9DA CRC64;
     MSKTRVYELA KELNLSSKDL ISKLNDLDIK VKNHMSTLED EEVELIMDLL RDKPQQTEEV
     HQKEEEDIFE DNLEDIEEER VYKKSFKKGS KKNKKNNKKA VLTEEKEEDE IKIITIPEFL
     TVKELAEKMK VNPTEIIKKL IAKGIMVTVN QQIDFENAAK IAEEYGFLVD KEEVKDELEM
     LLEETPDDEK DLQPRPPIVT VMGHVDHGKT SLLDAIRNTN VTMKEMGGIT QHIGASVVEI
     NDKKIVFLDT PGHEAFTAMR ARGASITDIV VLVVAADDGV MPQTVEAINH VKAANVPMIV
     AINKIDLPTA NPDRVKTELS ELGLVPEEWG GNTICVPVSA KKNIGIDNLL EMILLVAEME
     DLKANPNKPA RGTIIEAKLE KGKGPVATVI VQNGTLQIGD AILAGTVYGK VRAMLDDKGR
     RIKKAGPSMP VEVLGFSEVP EAGDKLIVVE DEKKARELAE RRKELQKEME LKRKQKVSLE
     DLFSQIQEGS VKELNIIIKA DVQGSVEALK KSIEDLSNEE VRIKVIHGAV GAITETDVML
     ASASNAIIIG FNVRPETNAK NLAEKEKVDI KLYRIIYEAI EDIKAAMKGL LEPKYKEVEL
     GRAEVRAVFR VPGVGNVAGC YVLSGKILRN SDIRVVRDGI VVYEGKIASL KRFKDDVREV
     QQGFECGIGI DRFNDIKEGD IIEAYQMEEI PR