ID   IF2_RICCK               Reviewed;         833 AA.
AC   A8EYF4;
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=A1E_02210;
OS   Rickettsia canadensis (strain McKiel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=293613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=McKiel;
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 canadensis.";
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; CP000409; ABV73387.1; -; Genomic_DNA.
DR   RefSeq; WP_012148585.1; NC_009879.1.
DR   AlphaFoldDB; A8EYF4; -.
DR   SMR; A8EYF4; -.
DR   STRING; 293613.A1E_02210; -.
DR   PRIDE; A8EYF4; -.
DR   EnsemblBacteria; ABV73387; ABV73387; A1E_02210.
DR   KEGG; rcm:A1E_02210; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000007056; 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..833
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008323"
FT   DOMAIN          331..501
FT                   /note="tr-type G"
FT   REGION          340..347
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          365..369
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          387..390
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          441..444
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          477..479
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         340..347
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         387..391
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         441..444
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   833 AA;  91534 MW;  97FA5D0B1B199B8D CRC64;
     MTDNQEIKPK KLTLGNSKLS LNKSFDSLTG AQSFVNAKSK TLVEVRKSSI GSTTTISLNK
     ERNNLDQTVI DANKEEFNRR LSILKKAAEQ SKLNDPSQIS TLSKLASINQ STNLKIETLE
     TDKEVAQKRQ NITENKVEVS AKIVQGDEDI LSQIYKKKAE TFVKSPLVGM RTRYSIESEK
     ESDKTAESKV VVQKIKLEEP KKFKKVDLFN MLSDDESGSG RTRTRSLASI KRAREKEKRK
     LVLQAPEKVY REVTIPEVIG VGDLANAMSE RVADVIKELM NLGILANASQ VIDADTAELV
     ATNLGHKVKR VQESDVENVL ISDDKVEDLR TRAPVVTVMG HVDHGKTSLL DALKSTDIAA
     GEIGGITQHI GAYRVTLADG RAITFIDTPG HEAFSEMRSR GTKVTDIAII VVAADDGIKT
     QTVEAINHAK VAGVPIIIAI NKIDKPNIDI ERVKNELYIH EIIGEEAGGD VMVIPISALK
     KINLDKLEEA ILLIAEMQDL KASPFGSAAG VVIESKIEKG RGTLTTILVQ RGTLKNGDII
     IAGTSYGKVK KMTNDKGLEI AEATPSVPVE IQGLNEVPFA GVKFNVVQNE KQAKDIAEYR
     MRLAKEKKIS IAPRSSLEDL FLKASGNSKI KELPLIIKGD VHGSVEAILG SLLKLPSDEI
     KLRILHSGVG PITESDISLA HASSAIIVGF NVRAGVNALT AAEKAKIDIR YYSIIYNLID
     DVKAIMSGML DPIVREQYIG SVEIRRVFNV TKVGKIAGSY VTKGIIKKGA DVRLLRDNIV
     IHEGKLKTLK RFKDEVKEVR EGYECGIAFE NYEDIRENDV VEVFELIQEQ RQL