ID   IF2_THEM4               Reviewed;         692 AA.
AC   A6LP48;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tmel_1865;
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=391009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429;
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., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., 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 Thermosipho melanesiensis BI429.";
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; CP000716; ABR31699.1; -; Genomic_DNA.
DR   RefSeq; WP_012058057.1; NC_009616.1.
DR   AlphaFoldDB; A6LP48; -.
DR   SMR; A6LP48; -.
DR   STRING; 391009.Tmel_1865; -.
DR   EnsemblBacteria; ABR31699; ABR31699; Tmel_1865.
DR   KEGG; tme:Tmel_1865; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001110; 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.
FT   CHAIN           1..692
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008367"
FT   DOMAIN          184..352
FT                   /note="tr-type G"
FT   REGION          193..200
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          218..222
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          239..242
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          293..296
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          330..332
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..200
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         239..243
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         293..296
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   692 AA;  78185 MW;  DDE0E93F7BE64191 CRC64;
     MARLRVYELA RQLEMDTRDL MKELKELGIE VKSHMSYIDE ETVNLLLEMY SEEDELEDEL
     IYEEYEEEVE KEIKRKSKEF VEKSEVVKKK KGVIKLEEED LKLDKFAQKI GIPQNRIIQD
     FFMKGEILKP GQTLNLQLAK KIAKIYDIKI SFEVEEREEK KVNPLEEVER YFEEKYSEGE
     GLSERPPVVT VMGHVDHGKT TLLDYIRNTR VAEREEGGIT QSIGAYQVEV NGKKITFIDT
     PGHEIFTEMR ARGAQATDIV VLIVAADDGV MPQTVEAFNH AKSANVPIIV AINKIDKPNA
     NVEKTKQELV NKINLIPEEW GGDTIVVPIS AKKGQNVDTL LEMILLVAEM QEIKGLPDGP
     VRAVTIETRM ERGFGPVANV IIKDGVLHVG DYVISGKVMG KVKALVNDRG ERIREAGPSM
     PVMIVGFEEL PDSHGMVYSV ESLSKAREIT SKIAELEQKE LRRKRHMKLE EILKMMEQSD
     RKELNLILKA DTNGSVLALN GAINKLQSDE IKINVIHSGV GAITSSDVML ATASDAIIFG
     FRVKADSKAR KMAEAEGIQI KTYSIVYKLI EDLKAALEGM LEPEEIEEIS GRGEIRKVFK
     IKKVGSIAGV QMKEGYVESD GIVRLYREGK LIFEGKIESL KHYQQDVKKV EAPQECGIKL
     EAFDDIKEGD ELEFYILKKV SKKLNFDEEK GE