ID   IF2_MYCMO               Reviewed;         600 AA.
AC   Q6KID8;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MMOB1520;
OS   Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS   mobile).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=267748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX   PubMed=15289470; DOI=10.1101/gr.2674004;
RA   Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA   Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA   Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA   Church G.M.;
RT   "The complete genome and proteome of Mycoplasma mobile.";
RL   Genome Res. 14:1447-1461(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; AE017308; AAT27638.1; -; Genomic_DNA.
DR   RefSeq; WP_011264672.1; NC_006908.1.
DR   AlphaFoldDB; Q6KID8; -.
DR   SMR; Q6KID8; -.
DR   STRING; 267748.MMOB1520; -.
DR   EnsemblBacteria; AAT27638; AAT27638; MMOB1520.
DR   KEGG; mmo:MMOB1520; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000009072; 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   PRINTS; PR00315; ELONGATNFCT.
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..600
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000232588"
FT   DOMAIN          112..279
FT                   /note="tr-type G"
FT   REGION          121..128
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          146..150
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          167..170
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          221..224
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          257..259
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         121..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         167..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         221..224
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   600 AA;  66505 MW;  58CF5A2D25487E6B CRC64;
     MAIKKAKRKS NVEEVKTQLL EIKTELKDGV FTFTGPMTIN EFSKKIKKQA KDVILHFFKQ
     GKMYNANQII NEEEIAELCL EFDYEFKKEE QITVSNFMDT LVLSDEAKDL EERAPIITVM
     GHVDHGKTTL IDVIRKSKIV DTEAGGITQH TGAYQIEYNG KKITFIDTPG HEAFTQMRSR
     GAKVTDIVIL VVAADDGVMP QTKEAIDHAK SANVPIIVFV NKMDKPNKDI DRILSALSTL
     DVVSEEWSGD TQFIYGSALK NQGIDKLFDA INLQAEILEL KANRNRDAIG TIIESHLDKG
     KGSVSVLIVQ NGTLTPRDFI VAGSQYGRIR SIEDTNGNSL DAAYPGTPVI VTGLNYVPNA
     GDRFIALSDE SFAKNIAEQK AFVDKQAELI SRNTIVVQDG IKVLNIILKA DVQGIAEAIK
     SKLLEIKNEE VKINVVRSSV GAITKSDILL AQASNAIIFG FNIRATGGIK TFAEESRVIV
     KTHTIIYELL DEVNELLNGL KAPKFKEVVT GEARIKKIFF YSKVGNIAGC EVISGKVTSG
     TKMRLIRNGI TVHEGILDSL QREKNQAREV LKGFEFGTHI KKFNDIKEDD IIQTFEDVQI