ID   IF2_RICB8               Reviewed;         828 AA.
AC   A8GW31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=A1I_03495;
OS   Rickettsia bellii (strain OSU 85-389).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=391896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU 85-389;
RA   Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT   "Complete genome sequencing of Rickettsia bellii.";
RL   Submitted (SEP-2007) 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; CP000849; ABV79058.1; -; Genomic_DNA.
DR   RefSeq; WP_012151818.1; NC_009883.1.
DR   AlphaFoldDB; A8GW31; -.
DR   SMR; A8GW31; -.
DR   PRIDE; A8GW31; -.
DR   KEGG; rbo:A1I_03495; -.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; NRDNRTG; -.
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.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..828
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008322"
FT   DOMAIN          326..496
FT                   /note="tr-type G"
FT   REGION          48..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..342
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          360..364
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          382..385
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          436..439
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          472..474
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        123..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335..342
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         382..386
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         436..439
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   828 AA;  90861 MW;  9C4F963B5A8F1E9D CRC64;
     MTDNQENKPK KLTLSNTKLS LNKSFDSLAS TQSFVNAKSK TLVEVRKSYS GSTTTLSLNK
     EKGSLETGSS SGSEEFNRRL SILKKAAEQS KLNDNSQIST LSKLASINQS IASQEDPIEV
     EQEESSDTNK VKEEPKIEEV KDIEESTLQT PKKKEDIFVK SPLVGTRTRY GIESEKTVDK
     VTENKVIAPK PKVEESRKFK KTDLFNMVGD DENDNRNRTR SLASIKRARE KEKRKSLVQV
     PEKVYREITL PEVIGVGDFA NAMSERVSDV IKELMKLGIL ANASQTIDAD TAELVATHLG
     HAVKRVQESD VENILITNDK EEDLRSRAPV VTVMGHVDHG KTSLLDALKS TDVASGETGG
     ITQHIGAYRV TLADGRAITF IDTPGHEAFS EMRSRGAGVT DIVIIVVAAD DGIKPQTVEA
     INHAKAANVP IIVAINKIDK PDIDIERIKN ELYMYEIIGE EAGGDVMVIP ISALKKINLD
     KLEEAILLIA EMQNLKASPF GSASGVVIES KIEKGRGALT TMLVQRGTLK SGDIIIAGTA
     YGKVKKMTND KGIEVLEATP SVPIEIQGLS HVPHAGDMFN VVQTEKQAKD IAEYRERVAK
     EKKISIAPRS SLEDLFLKAS GSSKIKELPL IIKGDVHGSV EAIAGSLLKL PNDEVKLRIL
     HSGVGPITES DVSLAHASSA IIVGFNVRAG ANAKTAAEKE KVEIRYYSII YDLLDDVKAI
     MSGMLDPIIR EQYIGSVEIR QIFNITKIGK IAGSYVTRGI IKKGAGVRLL RDNIVIHEGK
     LKTLKRFKEE VKEVREGYEC GIAFENYEDI REGDTVEVFE LIQEKKQL