ID   IF2_RICAH               Reviewed;         829 AA.
AC   A8GNW1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=A1C_04065;
OS   Rickettsia akari (strain Hartford).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=293614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hartford;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia akari.";
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; CP000847; ABV75086.1; -; Genomic_DNA.
DR   RefSeq; WP_012149717.1; NC_009881.1.
DR   AlphaFoldDB; A8GNW1; -.
DR   SMR; A8GNW1; -.
DR   STRING; 293614.A1C_04065; -.
DR   PRIDE; A8GNW1; -.
DR   EnsemblBacteria; ABV75086; ABV75086; A1C_04065.
DR   KEGG; rak:A1C_04065; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000006830; 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.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..829
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008321"
FT   DOMAIN          327..497
FT                   /note="tr-type G"
FT   REGION          336..343
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          361..365
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          383..386
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          437..440
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          473..475
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         336..343
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         383..387
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         437..440
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   829 AA;  90893 MW;  5A8EF35D99177FF4 CRC64;
     MTDNQEIKPK KLTLGNSKLS LNKSFDSLTG AQSFVNAKSK TLVEVRKSST GSTTTISLNQ
     ERNSLDHTAI DANKEEFNRR LSILKKAAEQ SKLNDTSQIS TLSKLASINQ SANSKIEPLE
     TDKEVEQKQQ NNEENKVEVS AKIVQDNEHI PSQISKKKEE SFVKSPLVGM RTRYGIELEK
     ELDKTADSKV VAPKIKLEEP KKFKKVDLFN MLGDDESGRT RSLASIKRAR EKEKRKLASQ
     APEKVYREVT IPEVIGVGDL ANAMSERVAD VIKELMKLGV LANASQTIDT DTAELVATNL
     GHTVKRVQES DVENVLISDD KVEDLRMRAP VVTVMGHVDH GKTSLLDALK STDIAASETG
     GITQHIGAYR VTLADGRAIT FIDTPGHEAF SEMRSRGAKV TDIVIIVVAA DDGIKTQTVE
     SINHAKAAGV PIIVAINKID KPDIDIERVK NELYVHEIIG EEAGGDVMVI PISALKKINL
     EKLEEAILLV AEMKDLKASP FGPASGVVIE SKIEKGRGTL TTILVQRGTL RNGDIIIAGS
     SYGKVKKMTN DKGLEIVEAT PSVPVEIQGL NEVPFAGDKF NVVQNEKQAK DIAEYRMRLA
     KEKKISIAPR SSLEDLFLKA SGNSKIKELP LIIKGDVQGS VEAILGSLLK LPSDAIKLRI
     LHSGVGPITE SDVSLAHASS AIIVGFNVRA GANALTAAEK EKVDIRYYSI IYNLIDDVKA
     IMSGMLDPIV REQYIGSVEI RQIFNITKVG KIAGSYVTKG IIKQGASVRL LRDNVVIHEG
     KLKTLKRFKD EVKEVREGYE CGIAFENYED IREGDTVEVF ELVQEQRQL