ID   IF2_EHRRG               Reviewed;         856 AA.
AC   Q5FGX3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=ERGA_CDS_04810;
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
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; CR925677; CAI27933.1; -; Genomic_DNA.
DR   RefSeq; WP_011255605.1; NC_006831.1.
DR   AlphaFoldDB; Q5FGX3; -.
DR   SMR; Q5FGX3; -.
DR   EnsemblBacteria; CAI27933; CAI27933; ERGA_CDS_04810.
DR   KEGG; erg:ERGA_CDS_04810; -.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; VIFAMNK; -.
DR   OrthoDB; 347113at2; -.
DR   BioCyc; ERUM302409:ERGA_RS02495-MON; -.
DR   Proteomes; UP000000533; 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..856
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228195"
FT   DOMAIN          356..526
FT                   /note="tr-type G"
FT   REGION          365..372
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          390..394
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          412..415
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          466..469
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          502..504
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         365..372
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         412..416
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         466..469
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   856 AA;  94957 MW;  5D69C51C52241232 CRC64;
     MNESKSVASN ELTSGKVERT TLKLSDKLKI SSNIQQGNKF SLNKSITTVE VRKSKKRKNI
     DEAARSSLLL QNNDIDGNSE DKNSLTIQEQ ISRMNALQNA SNNEKREELS SDSNKHIEEE
     VISVKAEVEQ PVDVVLPNDN LLIESDSSEK VIVDPVTDSE HADKDVQDVV MLDEFVSSNL
     DDAGDQKNGD QSDDISDLLE HKGIEGKKLK KYEKEHEEKK GNPKKVMSNN TYTKHVKLVI
     EEELEEDNNK QVIKNYRSKK NRVTNRSVKN KITRKVLIPN KITVQELANS MSERVKDVQQ
     VLYQITGKHD IKLTDYLDSD QASIIVEAFN HTFKLVDNAK LENDLYSDGN NMELIPRAPV
     VTVMGHVDHG KTSLLDAIRE SNVVDGEFKG ITQHIGAYQI TLNGDKKITF IDTPGHEAFA
     AMRAHGTNVT DIVVLVVAAD DGIMPQTIES INHVKAANVA MIVAVNKIDK HDADLDRITN
     ALLQHGVVAE SLGGDVIVVP VSAKEKINLD QLKSSILLIA DLLELKAVYN TRASGTVIES
     KVDKNCGVVA TLIVQKGTLK VGDIIVAGNQ AYGRVRNMFN ADGGSEKVAI PSMPVKVFGL
     NNVPNFGTSF IVVDSEKQAR ELINYRQDLL NVELSKQPAI DKSNVLLYDM VDELNVILKC
     DVMGSIEAIC YSIGKITHKD IRVNILYKGV GNITKSDVLL AETSNSIILA FNVKTDTQVK
     ELAKQKNIEI KHYFVIYDII DDIKKILTGM LKPLKQEVQI GTLSVRKVFS VGNNGSVLGC
     YVTSGLVKKG ALVKLVRNNN IIHEGKIKVL RRFKDDVKEV TAGFECGILL DYSKEIYPES
     DVMNIFEIVE EIRVIQ