ID   IF2_PSELT               Reviewed;         674 AA.
AC   A8F5A0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, 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}; OrderedLocusNames=Tlet_0768;
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX   NCBI_TaxID=416591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
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., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-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; CP000812; ABV33334.1; -; Genomic_DNA.
DR   RefSeq; WP_012002815.1; NC_009828.1.
DR   AlphaFoldDB; A8F5A0; -.
DR   SMR; A8F5A0; -.
DR   STRING; 416591.Tlet_0768; -.
DR   PRIDE; A8F5A0; -.
DR   EnsemblBacteria; ABV33334; ABV33334; Tlet_0768.
DR   KEGG; tle:Tlet_0768; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002016; 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..674
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000057662"
FT   DOMAIN          174..344
FT                   /note="tr-type G"
FT   REGION          183..190
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          208..212
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          229..232
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          283..286
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          320..322
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         183..190
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         283..286
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   674 AA;  75906 MW;  B814201D699933BC CRC64;
     MPRLRVYELA KKLNMSTKDL LQELEELGLN VKNHMSYIDE ETVGLLLEIF EEEEETAAKA
     KAAKPKKEKE ELEEIFQEVV LKPEDLQLNT LAVKIGVPLN RIIQDMFVKG IVLKPTQQID
     EKTAKDIAKI YGYRAKFYQP EEEISELETI ENELERLEKY FETLYETHKD ELSIRPPVVT
     VMGHVDHGKT TLLDKIRRTR VAEKEVGGIT QSIGAYQVVH KGKKITFIDT PGHELFTEMR
     AKGAQATDIV VLVVAADDGV MPQTIEAYNH AKVANVPVIV AINKIDKPNA NIEATKRQLV
     DKLNIIPEDW GGDTITVPIS ARTGHGIDEL LEMILLVAEL REIKCYPKGP ARCVIIESKL
     DRSLGPVANV IVKDGELRVG DYLVAGPTYC KVRILIDDKG KSIKIAEPSQ PVMIVGFEEV
     PDIRYSIYAV ESLESARTVT QQLKERLERD KMAKRRVRLE ELLKMMEESE KKELNLVLKA
     DTFGSLSAVQ NAIASLKSEE IKINIVHSGV GTVNNSDVML ASASNGIIVG FRVKVDAQAR
     KTAENEGIQI KTYEIIYDLL DNMKLALEGM LKPETVEELV GRGEIRKIFD IKKVGKIAGV
     QLLEGHVSKD CIVKVYRNGT FLFSDQIDSL KHYKEDVDKV SAPQECGLKL KSNEDLREND
     ELEFYEQHQV QKKL