ID   IF2_MESH2               Reviewed;         599 AA.
AC   Q5ZZV6;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
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=mhp601;
OS   Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT   swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(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; AE017332; AAV27988.1; -; Genomic_DNA.
DR   RefSeq; WP_011206432.1; NC_006360.1.
DR   AlphaFoldDB; Q5ZZV6; -.
DR   SMR; Q5ZZV6; -.
DR   STRING; 295358.mhp601; -.
DR   EnsemblBacteria; AAV27988; AAV27988; mhp601.
DR   KEGG; mhy:mhp601; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   PhylomeDB; Q5ZZV6; -.
DR   Proteomes; UP000006822; 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.
FT   CHAIN           1..599
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000232585"
FT   DOMAIN          111..278
FT                   /note="tr-type G"
FT   REGION          120..127
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          145..149
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          166..169
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          220..223
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          256..258
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         166..170
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         220..223
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   599 AA;  66818 MW;  B86A6B60BA0C9713 CRC64;
     MKKSQKRISN VSEIKAQLKT VETKVHNGVF LFSGIMTIAE LAQKINVSVN QIITYFFHQA
     KMYNLNHSLS EDEIAEICLE FGLDFKKEVQ IDASNFMEEV SILDQDKDLS PRPPIITVMG
     HVDHGKTTLL DYIRKTNIAK NEKGGITQHT GAYQVVFQGH IINFIDTPGH EAFTQMRARG
     AKVTDIIVLV VAADDGVMPQ TKEAINHAAA ANVPIIVFVN KMDKPNKDVD RIKNELSALN
     IVTEEWGGSN IFVYGSALTG QGIDTLFSSI LLLAEILELK ANKNRYPIGT VIEAKLHHNK
     GTIATLMVQN GTLMVRDFIV AGYQYGRIRS LENTNGQPIK FAPPGTPVIV TGLNYVPEAG
     DKFFGFHEEK FAKQLALERK QSEKISKTKV QTKQQTKEKT LNIIIKADVA GIAQALHSTI
     EKLASKQVHI HILHSGVGIV NKADILLAQT SNSIIYAFNL QIPAAIKAQA KQAQVEIREH
     TIIYKIVDEI KKQVRGMREI RYELQQIGTA KIIAKFWFSK VGSIAGCSVL SGKFVENCKI
     ELWRNSKLIH SGKIESLQRD KNPVKEVQVG NEFGTHIYKF NDIEIGDELK AFLDVEIEE