IF2_GEOTN
ID IF2_GEOTN Reviewed; 735 AA.
AC A4IMD7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=GTNG_1117;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO66491.1; -; Genomic_DNA.
DR RefSeq; WP_011887154.1; NC_009328.1.
DR AlphaFoldDB; A4IMD7; -.
DR BMRB; A4IMD7; -.
DR SMR; A4IMD7; -.
DR STRING; 420246.GTNG_1117; -.
DR EnsemblBacteria; ABO66491; ABO66491; GTNG_1117.
DR KEGG; gtn:GTNG_1117; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001578; 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..735
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008248"
FT DOMAIN 236..405
FT /note="tr-type G"
FT REGION 52..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..252
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 270..274
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 291..294
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 345..348
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 381..383
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 52..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 291..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 345..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 735 AA; 81496 MW; EAE159CE6A2152DB CRC64;
MSKMRVYEYA KKHNVPSKDV IHKLKEMNIE VNNHMTMLEA DVVEKLDHQY RVNSEKKAEK
KTEKPKRPTP AKAADFADEE MFEDKKETAK AKPAKKKGAV KGKETKKTEA QQQEKKLFQA
AKKKGKGPMK GKKQAAPASK QAQQPAKKEK ELPKKITFEG SLTVAELAKK LGREPSEIIK
KLFMLGVMAT INQDLDKDAI ELICSDYGVE VEEKVTIDET NFETIEIVDA PEDLVERPPV
VTIMGHVDHG KTTLLDAIRH SKVTEQEAGG ITQHIGAYQV TVNGKKITFL DTPGHEAFTT
MRARGAQVTD IVILVVAADD GVMPQTVEAI NHAKAANVPI IVAINKMDKP EANPDRVMQE
LMEYNLVPEE WGGDTIFCKL SAKTQDGIDH LLEMILLVSE MEELKANPNR RALGTVIEAK
LDKGRGPVAT LLVQAGTLKV GDPIVVGTTY GRVRAMVNDS GRRVKEAGPS MPVEITGLHD
VPQAGDRFMV FEDEKKARQI GEARAQRQLQ EQRSVKTRVS LDDLFEQIKQ GEMKELNLIV
KADVQGSVEA LVAALQKIDI EGVRVKIIHA AVGAITESDI LLATTSNAIV IGFNVRPDTN
AKRAAESENV DIRLHRIIYN VIEEIEAAMK GMLDPEYEEK VIGQAEVRQT FKVSKVGTIA
GCYVTDGKIT RDSKVRLIRQ GIVVYEGEID SLKRYKDDVR EVAQGYECGV TIKNFNDIKE
GDVIEAYIMQ EVARA
