IF2_THET2
ID IF2_THET2 Reviewed; 571 AA.
AC Q72KE8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=TT_C0347;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS80695.1; -; Genomic_DNA.
DR RefSeq; WP_011172797.1; NC_005835.1.
DR AlphaFoldDB; Q72KE8; -.
DR SMR; Q72KE8; -.
DR STRING; 262724.TT_C0347; -.
DR PRIDE; Q72KE8; -.
DR EnsemblBacteria; AAS80695; AAS80695; TT_C0347.
DR GeneID; 3168456; -.
DR KEGG; tth:TT_C0347; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000592; 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..571
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228255"
FT DOMAIN 71..239
FT /note="tr-type G"
FT REGION 80..87
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 105..109
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 126..129
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 180..183
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 216..218
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 80..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 126..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 180..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 571 AA; 63178 MW; 7FA1269583DB969F CRC64;
MAKVRIYQLA KELGMETQEL LELLDQMGVA YKSHASTLEE KDAEAVRELV KEQRGLQEKL
AEEERRKSLP RRPPVVVIMG HVDHGKTTLL DYLRKSRIAE KEAGGITQHV GAFEVKTPQG
TVVFIDTPGH EAFTTIRQRG AKVADIAVIV IAADDGIMPQ TEEAIAHAKA AGAKLIFAIN
KIDLPQADPE KVKRQLMERG FVPEEYGGDA IVIPISAKTG QGVQDLLEMI LLLAELEDYR
ADPNAEPRGV ILESKLDKQA GIIANMLVQE GTFRVGDYVV AGEAYGRIRA MMDADGNQRK
EAGPGSAVQV LGFQELPHAG DVVEWVPDLE AAKEIAEERK EERKAREEEE KARRPRTMAE
LLRAMQEEGR KELNLILRAD TQGSLEAIQH ILARESTEDV KINILLAQVG APTESDVLLA
QTANAAILAF GVNPPGSVKK KAEEKGVLLK TFRIIYDLVD EVRNMVKGQR EPQYKEEVLG
QAEVRAIFRL PTGKQVAGCM VTQGRIPRNA EVRVLRDGQV IWQGRIASLK RFKEDVREVA
QGYECGIGLD GFDDFREGDV IEAFQMVEVP A