ID   IF2_MYCMS               Reviewed;         620 AA.
AC   Q6MTQ0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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=MSC_0349;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
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; BX293980; CAE76986.1; -; Genomic_DNA.
DR   RefSeq; NP_975344.1; NC_005364.2.
DR   AlphaFoldDB; Q6MTQ0; -.
DR   SMR; Q6MTQ0; -.
DR   STRING; 272632.MSC_0349; -.
DR   EnsemblBacteria; CAE76986; CAE76986; MSC_0349.
DR   KEGG; mmy:MSC_0349; -.
DR   PATRIC; fig|272632.4.peg.377; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001016; 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..620
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228215"
FT   DOMAIN          119..288
FT                   /note="tr-type G"
FT   REGION          128..135
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          153..157
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          175..178
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          229..232
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          265..267
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         175..179
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         229..232
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   620 AA;  68802 MW;  D77BCDD8E12C57A1 CRC64;
     MKKQVKNIKK QKAQNQTKNI KKQLKEEVNT GLIDGIFVYT EPLSVIEFAT KINKPLTAIL
     KHYFNQGLLL NQNTLLTEEQ MGELCLEFGF DFKKETTVTK ENILQTLLET VDDEKHLKER
     PPIVTIMGHV DHGKTTLLDS IKNSNVVASE AGGITQAIGA YQITTNHNKK ITFIDTPGHE
     AFTEMRSRGA NVTDIVVLIV AADDGVMPQT EEAIDHAKLA NVPIIVFINK IDKPEADPNR
     VKTELMKYGL VAEEFGGDIP FIEGSAIKKI NLDKLQDTII LISELENLKA NPDKFASGVV
     LEAHLDKAKG PVASVLVQQG TLEIKDIMIA GTTFGSIKHI EDEFKHKVLK AEPSKPVVVY
     GLNQVPKAGD KFVVINDEKM AREISEAQLK KQQEEERRTK QAFTLDAIKQ HIDEGELKNI
     TLIIKADTQG SVEALKNSLS KINISGVKIN IIRASVGAIS LSDISLASTV RDGLVIVYGF
     NVRPDAIVRK KAEEDHIEIK LHNIIYKVIE ELEDAAKGIL DPEVKELVLG QAQVRALFRH
     SAIGTIGGFY VLDGIIPRNA KIRVIRNGVV VYDGEINSLQ HQKQDAKEIK AGFEGGLTIK
     NFNDIKEEDI FEAYKIEQIK