ID   IF2_MYCPU               Reviewed;         603 AA.
AC   Q98R05;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MYPU_2050;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL445563; CAC13378.1; -; Genomic_DNA.
DR   PIR; E90537; E90537.
DR   RefSeq; WP_010925009.1; NC_002771.1.
DR   AlphaFoldDB; Q98R05; -.
DR   SMR; Q98R05; -.
DR   STRING; 272635.MYPU_2050; -.
DR   PRIDE; Q98R05; -.
DR   EnsemblBacteria; CAC13378; CAC13378; CAC13378.
DR   KEGG; mpu:MYPU_2050; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   BioCyc; MPUL272635:G1GT6-207-MON; -.
DR   Proteomes; UP000000528; 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..603
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000232590"
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   603 AA;  67855 MW;  CA23E342F0C27957 CRC64;
     MAKKRDKRLS NINEIKTQII NVKTELKNGV FIFSSPMTIG EFAQKINISG TEIVKEYFLK
     GKMYTLNHIL SEEEIADLCF KHGYDFRVEK EINASNFLDN IEFEDKKEDL ETRPPIITIM
     GHVDHGKTTL IDKIRKSNIV STESSGITQH TGAYQIIYDN KKITFLDTPG HEAFSAMRAR
     GSKVTDIVIL VVAADDGVKP QTKEAIAHAQ AANVPIIVFV NKMDKPSKDL NRLKNDLSVS
     GINLEEWGGD TPIVYGSALK GEGIEKLFEN INLQAEILDL KFNPKRHPLG VVIESKMDKG
     VGSLTTVIVQ NGTLHKGDFL VAGPRYGRVK AIYDTNKKPL KKVGAGTPVF VIGLNYAPSA
     GEKFVGINDE KYAKKLSQER EDSEKQEKFL QQTQTISIRR DNDKKIFNII IKSDTQGTAE
     AIKDLILQIA NDEIEVIVVS YGIGVINNSD LLLAQTSNSE IIGFNSKPNP NIKQQAEDLN
     IQINSFDVVY KIVDYLNEKI NKMVKPKFEK RTIGRAKILK VFFYSKVGNI AGCLMEEGHV
     KSDSFVKVYR KNKLIHDGRV ETLRKGPDEV KKIEKGFEFG LRIKNFDDIK EDDQLEIIEE
     FRI