ID   IF2_MALP2               Reviewed;         620 AA.
AC   Q8EWU0;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, 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=MYPE1110;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC43903.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8EWU0; -.
DR   SMR; Q8EWU0; -.
DR   STRING; 272633.26453571; -.
DR   EnsemblBacteria; BAC43903; BAC43903; BAC43903.
DR   KEGG; mpe:MYPE1110; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002522; 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..620
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000232589"
FT   DOMAIN          126..295
FT                   /note="tr-type G"
FT   REGION          135..142
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          160..164
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          181..184
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          235..238
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          271..273
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         181..185
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         235..238
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   620 AA;  68954 MW;  77395C20303C89BA CRC64;
     MEVFMAKNVK TKSKNKNKKI VDNRTNIDIK SQFKKVETGI KNGVFVFTNN LTIDEFSKKI
     NKHSAEIIKY LFLKGINCNL NTLLDERQMG ELCLEFGYDF KKEIQINEDN FLDNIKFEDR
     EDLLDKRPPI VTIMGHVDHG KTTLLDTIRK SKVAATEAGN ITQSIGAYQV EWKKHLITFF
     DTPGHEAFSK MRAVGADLTD IVVLVVAADD GLKPQTEEAI DHALFAKAPI IVFINKMDKK
     DANIEKIYSQ LAEKNVLCEE WGGKTMVIKG SALNNQGIDE LLEAIIVTAE IMELKANPKR
     LANGITIEAS MDKGEGAVAD LLVQSGTLAV NDYILVGEYY GKVKKMVDFN RKEIKTALPS
     TPVRISGLNG IPKSGDKWIV TNDEKLLKEL SEKRQLNTKQ RKLSNFGTNL NENSQGIKEL
     NVILKTDNNG SLEAIKGLLS SIEVTGAKLN LVRAAIGSIN ESDIDLARTS KSLVVIFNTK
     VSSKVSDYAI SMGITIKNYN IIYQIKDEIE RLLKGILDPV FVEKEIGSVE IRQLWSHSSI
     GVIAGGRVLT GEIKRNAFAR IKRKDKEIIS NAKINSLRHG KDSIASAAAG KECGFTLENF
     NDFVEGDIVE IYEIVGETHE