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IF2_BLOFL
ID   IF2_BLOFL               Reviewed;         897 AA.
AC   Q7VQM3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bfl104;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83625.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7VQM3; -.
DR   SMR; Q7VQM3; -.
DR   STRING; 203907.Bfl104; -.
DR   PRIDE; Q7VQM3; -.
DR   EnsemblBacteria; CAD83625; CAD83625; Bfl104.
DR   KEGG; bfl:Bfl104; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002192; 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; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF46955; SSF46955; 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; Reference proteome.
FT   CHAIN           1..897
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137185"
FT   DOMAIN          402..570
FT                   /note="tr-type G"
FT   REGION          411..418
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          436..440
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          458..461
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          512..515
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          548..550
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         411..418
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         458..462
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         512..515
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   897 AA;  100775 MW;  D2DAFEF1557A7D15 CRC64;
     MTIQSFAIEV QMSVDYLIQQ FLDIGITKTK FDFITQSEKE ILFRHMNVNK IAVFNKLFLQ
     RKTHSTLNVS STNGKSKKVK VEVRKKRVYM VPCSIRKSHV SNNTNILLVE NDNSKDKYKS
     DDCNELSELV ACDENKISSN ENQVMCFISQ KEKLDHFTIR QDYVRTNELV KDVNQDLDHQ
     IRDRKGLSNS VCCDVLLNVQ DEQHDDNNFS CGLSDDMAVS NNIPEHDKQK LENVRKNLTD
     RLRSTRTRNL SKLVKQNKHN NSKVCMIYES DKDEKLYVLP SSRVYKNKRK QSILVQSFNK
     PMQKTVRDVV IGETISVAEL SNKMSIKSSS MIKMMMKLGL MVTINQNLDQ ETAQLVVEEM
     GHNAILRREN ALEELIMHDN NNDYQNISSK LDNAKNDMGY KNRAPIVTIM GHVDHGKTSL
     LDYIRSTNVA SSESGGITQN IGAYCVQLAN NDMVTFIDTP GHEAFTDMRA RGIQLTDIVV
     LVVAADDGVM PQTVEAIQYI RDGNLPVIIA INKIDKSVTN VERIKNELNS YGFIPEEWGG
     HTQFVNVSAV SGEGVNDLLD SILVQSEILE LKSMHHGLAK AVVIESSLDR SRGPVVTVLV
     RSGELKCGDI VLCGTEYGRV RAMRDSLGFD VIKAGPSIPV ELLGLSGIPG TGEWLVVVNN
     EKKAREVALY RKEKKREIKL ARKSEKTIIE NFNSMDIIKI KELNFIIKSD TQGSMEVICE
     SLKKLSTNKM VMKILSASIG NVTETDAVLA LSSHSRILAF NVKVDLSAKN IIELNHINIQ
     YYSVIYSLLD EVKELISSTI APQVDFKVIG IAKVHNIFQS PRYGTIAGCM VTQGVIKLHK
     QIKIVRNGII MYKGVLDSLR HFKNDVSEVK IGVECGIGIK NYSDVCSGDI IEVLDKI
 
 
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