ID   IF2_MESFL               Reviewed;         629 AA.
AC   Q6F1H1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-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=Mfl295;
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC   Mesoplasma.
OX   NCBI_TaxID=265311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE017263; AAT75652.1; -; Genomic_DNA.
DR   RefSeq; WP_011183192.1; NC_006055.1.
DR   RefSeq; YP_053536.1; NC_006055.1.
DR   AlphaFoldDB; Q6F1H1; -.
DR   SMR; Q6F1H1; -.
DR   STRING; 265311.Mfl295; -.
DR   PRIDE; Q6F1H1; -.
DR   EnsemblBacteria; AAT75652; AAT75652; Mfl295.
DR   GeneID; 2898273; -.
DR   KEGG; mfl:Mfl295; -.
DR   PATRIC; fig|265311.5.peg.295; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000006647; 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..629
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228212"
FT   DOMAIN          127..297
FT                   /note="tr-type G"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..143
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          161..165
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          183..186
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          237..240
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          273..275
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         183..187
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         237..240
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   629 AA;  68990 MW;  FC26B6AD8BF5D604 CRC64;
     MAKNIKTNKK PQQVNKKEMS KQHAKQIKQQ LNETVATGII DGVFVYTEAL SIADFANQIG
     KSVAEILKYF FAQGLMLNQN VVLSEEQMAE LALEFGFDFR KEESLTKENF FEALDASEED
     KPEDLEHRAP IVTIMGHVDH GKTTLLDSIK NTNVVGGEAG GITQAIGAYQ VKNKDGKKIT
     FIDTPGHEAF SEMRSRGANV TDIVILIVAA DDGVMPQTEE AIDHAKLANV PIIVFINKCD
     KPGADPERVK AELMKYEIVA EEYGGDIPFV QGSAKQKIGL DQLEETILLI AEMQDYKANP
     NKLAKGVVIE AHLDKAKGPV ASILVKEGTL DIRDMIIAGT TYGNIKHMED ETNKKVLKAG
     PSKPVVVYGL NEVPSAGDKF IVMNDEKMAR TIAEAQAEKK LAAERQSNQI FSLDSIKKHI
     DDGELKAINL IVKADTQGSV EALKGSLTKI DIPGVKLNII RASVGTITLS DVTLASTVTD
     GIVLIYGFNV RPDAVVRKKA EEEGIEIRLH NIIYKVIEEL EDAAKGMLDP EYKEVVTGSA
     EIRATFKHSD IGTIGGFHIT DGSIERKSKV RIIRNGIVIY TGELATLKHL KDDIKEAKIN
     SEGGLTIKNF NDIKEGDIVE GYKEEEVKK