ID   IF2_THEP3               Reviewed;         691 AA.
AC   B0K9Q0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Teth39_1209;
OS   Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS   thermohydrosulfuricum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=340099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33223 / DSM 2355 / 39E;
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., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA   Richardson P.;
RT   "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000924; ABY94863.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0K9Q0; -.
DR   SMR; B0K9Q0; -.
DR   STRING; 340099.Teth39_1209; -.
DR   EnsemblBacteria; ABY94863; ABY94863; Teth39_1209.
DR   KEGG; tpd:Teth39_1209; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002156; 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; Reference proteome.
FT   CHAIN           1..691
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093838"
FT   DOMAIN          193..362
FT                   /note="tr-type G"
FT   REGION          202..209
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          227..231
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          248..251
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          302..305
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          338..340
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         248..252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         302..305
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   691 AA;  76823 MW;  F1870EC74D70DE0E CRC64;
     MSKTRVYELA KELNLSSKDL ISRLNDLDIK VKNHMSTLED EEVDLIMDLL SDKPQQTDEI
     NQQEEDIFED NLEDLEEERA YKKSFKKGGK KNKKNNKKVI LTEEKQEDEI KIITIPEFLT
     VKELAEKMKV NPTEIIKKLI AKGIMVTVNQ QIDFENASKI AEEYGFLVDK EEVKDELELL
     LEEAPDDEKD LQPRPPIVTV MGHVDHGKTS LLDAIRNTNV TMKEMGGITQ HIGASVVEVN
     NKKIVFLDTP GHEAFTAMRA RGASITDIVV LVVAADDGVM PQTVEAINHV KAANAPMIVA
     INKIDLPTAN PDKVKTELSE LGLVPEEWGG NTICVPVSAK KNIGIDNLLE MILLVAEMED
     LKANPNKPAR GTIIEAKLEK GKGPVATVIV QNGTLQIGDA ILAGTTYGRV RAMFDDKGKR
     IKKAGPSTPV EVLGFSEVPE AGDKLIVVEE EKKARELAER RKELQKEMEL KRKQKVSLED
     LFSQIQEGSV KELNIIIKAD VQGSVEALKK SIEDLSNEEV RIKVIHGAVG AITETDVMLA
     SASNAIIIGF NVRPETNAKN LAEKEKVDIK LYRIIYDVIE DIKAAMKGLL EPKYKEVELG
     RAEVRAVFRV PGVGNVAGCY VLSGKILRNA DVRIIRNGIV VYEGKIASLK RFKDDVREVQ
     QGFECGIGIE KFNDIKEGDI IEAYQMEEIP R