IF2_THEPX
ID IF2_THEPX Reviewed; 692 AA.
AC B0K1D6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Teth514_1645;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) 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; CP000923; ABY92931.1; -; Genomic_DNA.
DR AlphaFoldDB; B0K1D6; -.
DR SMR; B0K1D6; -.
DR EnsemblBacteria; ABY92931; ABY92931; Teth514_1645.
DR KEGG; tex:Teth514_1645; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002155; 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; 2.
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..692
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093839"
FT DOMAIN 194..363
FT /note="tr-type G"
FT REGION 203..210
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 228..232
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 249..252
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 303..306
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 339..341
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 203..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 249..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 303..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 692 AA; 77133 MW; 9D6561586503B9DA CRC64;
MSKTRVYELA KELNLSSKDL ISKLNDLDIK VKNHMSTLED EEVELIMDLL RDKPQQTEEV
HQKEEEDIFE DNLEDIEEER VYKKSFKKGS KKNKKNNKKA VLTEEKEEDE IKIITIPEFL
TVKELAEKMK VNPTEIIKKL IAKGIMVTVN QQIDFENAAK IAEEYGFLVD KEEVKDELEM
LLEETPDDEK DLQPRPPIVT VMGHVDHGKT SLLDAIRNTN VTMKEMGGIT QHIGASVVEI
NDKKIVFLDT PGHEAFTAMR ARGASITDIV VLVVAADDGV MPQTVEAINH VKAANVPMIV
AINKIDLPTA NPDRVKTELS ELGLVPEEWG GNTICVPVSA KKNIGIDNLL EMILLVAEME
DLKANPNKPA RGTIIEAKLE KGKGPVATVI VQNGTLQIGD AILAGTVYGK VRAMLDDKGR
RIKKAGPSMP VEVLGFSEVP EAGDKLIVVE DEKKARELAE RRKELQKEME LKRKQKVSLE
DLFSQIQEGS VKELNIIIKA DVQGSVEALK KSIEDLSNEE VRIKVIHGAV GAITETDVML
ASASNAIIIG FNVRPETNAK NLAEKEKVDI KLYRIIYEAI EDIKAAMKGL LEPKYKEVEL
GRAEVRAVFR VPGVGNVAGC YVLSGKILRN SDIRVVRDGI VVYEGKIASL KRFKDDVREV
QQGFECGIGI DRFNDIKEGD IIEAYQMEEI PR