IF2_THET8
ID IF2_THET8 Reviewed; 571 AA.
AC P48515; Q5SKE4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=TTHA0699;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9030723; DOI=10.1111/j.1432-1033.1997.66_1a.x;
RA Vornlocher H.-P., Scheible W.R., Faulhammer H.G., Sprinzl M.;
RT "Identification and purification of translation initiation factor 2 (IF2)
RT from Thermus thermophilus.";
RL Eur. J. Biochem. 243:66-71(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z48001; CAA88038.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70522.1; -; Genomic_DNA.
DR PIR; S52276; S52276.
DR RefSeq; WP_011172797.1; NC_006461.1.
DR RefSeq; YP_143965.1; NC_006461.1.
DR PDB; 3J4J; EM; 11.50 A; A=1-569.
DR PDB; 4B3X; X-ray; 1.95 A; A=1-363.
DR PDB; 4B43; X-ray; 1.94 A; A=1-363.
DR PDB; 4B44; X-ray; 2.70 A; A=1-363.
DR PDB; 4B47; X-ray; 2.30 A; A=1-363.
DR PDB; 4B48; X-ray; 2.80 A; A=1-363.
DR PDB; 4KJZ; X-ray; 2.80 A; A/B/C/D=2-474.
DR PDB; 5LMV; EM; 4.90 A; a=1-571.
DR PDBsum; 3J4J; -.
DR PDBsum; 4B3X; -.
DR PDBsum; 4B43; -.
DR PDBsum; 4B44; -.
DR PDBsum; 4B47; -.
DR PDBsum; 4B48; -.
DR PDBsum; 4KJZ; -.
DR PDBsum; 5LMV; -.
DR AlphaFoldDB; P48515; -.
DR SMR; P48515; -.
DR STRING; 300852.55772081; -.
DR EnsemblBacteria; BAD70522; BAD70522; BAD70522.
DR GeneID; 3168456; -.
DR KEGG; ttj:TTHA0699; -.
DR PATRIC; fig|300852.9.peg.693; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; P48515; -.
DR BRENDA; 3.6.5.3; 2305.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding;
KW Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..571
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137273"
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:0000250"
FT BINDING 126..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 180..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 319
FT /note="A -> P (in Ref. 1; CAA88038)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> G (in Ref. 1; CAA88038)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4B48"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 40..66
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4KJZ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4B47"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4B3X"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:4KJZ"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4B43"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4B43"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 223..237
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:4KJZ"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:4B43"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 307..315
FT /evidence="ECO:0007829|PDB:4B43"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:4B43"
FT HELIX 329..351
FT /evidence="ECO:0007829|PDB:4B43"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:4KJZ"
FT STRAND 372..380
FT /evidence="ECO:0007829|PDB:4KJZ"
FT TURN 383..387
FT /evidence="ECO:0007829|PDB:4KJZ"
FT HELIX 388..392
FT /evidence="ECO:0007829|PDB:4KJZ"
FT STRAND 401..411
FT /evidence="ECO:0007829|PDB:4KJZ"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:4KJZ"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:4KJZ"
FT TURN 436..439
FT /evidence="ECO:0007829|PDB:4KJZ"
FT HELIX 440..444
FT /evidence="ECO:0007829|PDB:4KJZ"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:4KJZ"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:4KJZ"
FT TURN 465..469
FT /evidence="ECO:0007829|PDB:4KJZ"
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
