ID   IF2_OCEIH               Reviewed;         692 AA.
AC   Q8EQU1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=OB1598;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13554.1; -; Genomic_DNA.
DR   RefSeq; WP_011065998.1; NC_004193.1.
DR   AlphaFoldDB; Q8EQU1; -.
DR   SMR; Q8EQU1; -.
DR   STRING; 221109.22777281; -.
DR   PRIDE; Q8EQU1; -.
DR   EnsemblBacteria; BAC13554; BAC13554; BAC13554.
DR   KEGG; oih:OB1598; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   PhylomeDB; Q8EQU1; -.
DR   Proteomes; UP000000822; 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..692
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137229"
FT   DOMAIN          193..362
FT                   /note="tr-type G"
FT   REGION          51..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   COMPBIAS        59..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   692 AA;  76147 MW;  733888FBEFA8D639 CRC64;
     MSKIRIYEYA KQNNLASKDV INFLKTENVE VSNHMSAISD EVVKKLDNKF KAKPENAKKG
     QNQKQSNNQQ QNRQKQNQKN QSKPNKNKKQ KGPKKNQQQE RPAAKPAETP GKITYHGTLT
     VQDLAGKLNK EPAELIKKLM FLGVMATKNQ DIDDDAIELI CGEYDVEVEK EIILEDTDLD
     KYIEEDAEEN LQERPAVVTI MGHVDHGKTT LLDSIRHTKV TAGEAGGITQ HIGAYQVEND
     GKKITFLDTP GHAAFTSMRS RGAQVTDIAI LVVAADDGVM PQTVEAINHA KAAEVPIIVA
     VNKMDKEGAN PDRVMQELTE HQLIPEDWGG NTIFVNLSAI KNEGIDDLLE MILLVSEVEE
     LKANPNAKAF GSVIDAQLDK GRGSVATLLV QNGTLHVGDP LVVGSTFGKV RAMVNDLGNR
     VTEVGPSTPV EITGLHGVPQ AGDQFLVFKD EKKARQIGEA REQKQIDENR GTQSTVSLDD
     LFEQIKQGEM KELNIIVKAD VQGSVEALAA SLQKIEVEGV NVKIIHTGVG AITESDIILA
     SASKAIVIGF NVRPDVNAKN AAESEKVDLR LHRVIYNAIE EIESAMKGLL DPEYQEKVIG
     QAEVREIFKV SRIGTIAGSY VTDGKITRDA GVRLIRDGVV LYEGELQALK RFKDDVKEVQ
     TNYECGITIS NFNDIKEGDT IEAFVMEEIE RK