ID   IF2_MYCGA               Reviewed;         615 AA.
AC   Q7NBZ4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MYCGA1150;
GN   ORFNames=MGA_0821;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; AE015450; AAP56465.1; -; Genomic_DNA.
DR   RefSeq; WP_011113343.1; NC_004829.2.
DR   AlphaFoldDB; Q7NBZ4; -.
DR   SMR; Q7NBZ4; -.
DR   KEGG; mga:MGA_0821; -.
DR   PATRIC; fig|233150.7.peg.125; -.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001418; 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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..615
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137220"
FT   DOMAIN          118..285
FT                   /note="tr-type G"
FT   REGION          127..134
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          152..156
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          173..176
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          227..230
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          263..265
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         173..177
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         227..230
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   615 AA;  68086 MW;  422C80CBB42E5974 CRC64;
     MNKKPTRNKK PVDQRSKINI KSYLKEVQVG VKDGVFIYTD PLSIDQFAKK VNQPVAKIIK
     HFFSKGINTI NLNTILSLEQ IGELCLDLGL DFKIEKSVTS ENLLDNIEFK DKKEDLVKRP
     PIVTVMGHVD HGKTSLLDAI RSTNVTSNEA GGITQHIGAY QVKKNDELIT FIDTPGHEAF
     TEMRARGANL TDIVVLVVAG DDGIKPQTEE AIDHAKNANV PIIVFVNKMD KSGANFDRVI
     QQISKYDLSP EEYGGDTIFV QGSAIKKEGI NELLDAILTL AEINEYKANP NADPYGIVIE
     SKLEPGLGPQ ATVIIKRGTL KVGDYICIGA AYGKVRIMQD ENGNNLTEAT PSRPVKISGL
     DAIPQAGEKF LGLATEKEVK ELSDSYKLKQ QKQKHLSLQE SHEKRTRINT NGIKCVDLII
     KSDVQGSLEA IKYAISNINI EGVTTNIIRA STGVISETDI KLAQASNSTV ISFNLGVSKQ
     IRDLANSDNV QILSYEIIYK MVEDLEKIMK GELDPVYEES VIGQAVVRVL WKHSKIGTIA
     GSYVTSGKVV KNALCRVLRD DVIIYKSKIA SLKSKTTFVD KVEHNKECGI VVENYNDIKE
     DDIIEVYEIV KKRVY