ID   IF2_WIGBR               Reviewed;         841 AA.
AC   Q8D2X6;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=WIGBR2260;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(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; BA000021; BAC24372.1; -; Genomic_DNA.
DR   RefSeq; WP_011070030.1; NC_004344.2.
DR   AlphaFoldDB; Q8D2X6; -.
DR   SMR; Q8D2X6; -.
DR   STRING; 36870.25166181; -.
DR   PRIDE; Q8D2X6; -.
DR   EnsemblBacteria; BAC24372; BAC24372; BAC24372.
DR   KEGG; wbr:infB; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000562; 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; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF46955; SSF46955; 1.
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..841
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137283"
FT   DOMAIN          341..508
FT                   /note="tr-type G"
FT   REGION          350..357
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          375..379
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          396..399
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          450..453
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          486..488
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         350..357
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         396..400
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         450..453
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   841 AA;  94759 MW;  B693CC2705D050F7 CRC64;
     MKNVTIKSFS EEIKIPINKL IQKFADAGIT KTNIDYVSLE EKKILLSYIN SHHVNLPKNL
     SLQKKTKSKL NISSLNGKNK IVKIEVRKKK YLKCDSSLLF KDKIVKNNID KTFCKKNIKD
     LNKTKKYVEL SKNINEREIN FEKKLIKEPI LDKSKLKISK NLIKKNVKIN KNLNIYKKNE
     FKQNLKKNKL NKKEKNKKIE INYKVKNKNE NIFKKIKSNR LFGSETNFFN NNIDKKTNIR
     KKISSLTHTF NKPLKKIIKE ITIGETISVF ELSNKMAVKS HKVVSNMMKL GIKSSINEVI
     DQDIAQIIAE EMGHKVKLIK NNALEEEIIK NQNKNLYELK NRAPVVTIMG HVDHGKTSLL
     DYIRTTKVAL KEKGGITQCI GAYYVKTKKG IITFIDTPGH AAFTEMRIRG SKITDIIVIV
     IAADDSIMPQ TVEAINHAKI AKVPVIIAIN KIDKITSNPE KVKKELIKHG IFLEEYGGDT
     QCLLISAKSG LGIDFLLDAI LLQAEILELK AMHKGMASGT VIESRLEKGK GPVSTILIQE
     GRLHQGDVVL CGCEYGKIKA MQDSFKCKIK SVGPSIPVEI LGLSGIPISG DKITVVKEEK
     KAREVAIYRQ NKLRESKLRI NKKIKIENVF SNLNLSTKKN INIVLKSDAH GSSQAISNAL
     ILLSNEEIKI NIIYSGVGPI TETDVALATS SNAIIIGFNV KPDFSNIKNT ESIGLNIKCC
     SIIYEIVDFV KQKIYLSCNT KYNKKIIGIL IVKNIFQLPK LGSIAGCIVK EGIVKKNSIA
     KILRNKSFVH ESKIISLRRF KEDVNEVKSG TECGIVIKNF NDIKPLDIIE ILELEELNKK
     I