IF2_CORGB
ID IF2_CORGB Reviewed; 1003 AA.
AC A4QEZ2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=cgR_1814;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(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; AP009044; BAF54808.1; -; Genomic_DNA.
DR RefSeq; WP_011897398.1; NC_009342.1.
DR AlphaFoldDB; A4QEZ2; -.
DR SMR; A4QEZ2; -.
DR PRIDE; A4QEZ2; -.
DR EnsemblBacteria; BAF54808; BAF54808; cgR_1814.
DR KEGG; cgt:cgR_1814; -.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OMA; QVRPEMI; -.
DR PhylomeDB; A4QEZ2; -.
DR Proteomes; UP000006698; 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 PRINTS; PR00315; ELONGATNFCT.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..1003
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008235"
FT DOMAIN 498..670
FT /note="tr-type G"
FT REGION 36..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..514
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 532..536
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 557..560
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 611..614
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 647..649
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 76..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 507..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 557..561
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 611..614
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1003 AA; 103374 MW; E55DD86B0829E7FC CRC64;
MPGKLRVHEL AKQLGITSKE LLATLKDKGE FVKTASSTIE PPVVKRMQEH YGSSGSDKSD
TAAKPAAAKP AAPKPAASAA PKPGAPAKPA APAAKPAPAA ASAAKPGAAP KPGVQAKPAA
AAKPGAPAKP AAPSAAKPGS APKPAAAAKP AFSGPTPGDA AKKAEPAAKP GAEAPRPDGM
PRPMGKPAPK PGARAPRVAN NPFSTGGGER PAPRPGGGPR PGGGPRPGGG PRPQGQGRPG
GQRDGQRDGQ RDGQGNRGGQ RQGAGAGGPR PQGGPRPQGG SRPQGGSAQG GSAKGAQGAP
SQERQGGGRR PSPAMMPPTP GQMPAKAPGK GGRGGQAGGG AGGGFNRGGG TGGGAGRGGR
RGGTAGAFGR PGGAPRRGRK SKRQKRNEYE SMQAPNVIGG VRLPDGKGAT IRLARGASLA
DFADKIGADA AALVQALFNL GEMVTATASV SDETLQLLGE EMNYKVQVVS PEDEDRELLE
SFDLQFGEDE GGEADLAKRP PVVTVMGHVD HGKTRLLDTI RKANVGSDEA GGITQGIGAY
QVKVNVEDTE RTITFLDTPG HEAFTAMRAR GAKSTDIAVL VVAADDGVMP QTVEAINHAK
AADVPIVVAV NKIDKPEASP EKIRGQLTEY GLIPEEYGGD TIFVDISAKQ GLNIDELLAS
VCLTADAELD LVANPEMDAQ GVAIEAHLDR GRGPVATVIV QRGTLRVGDS IVAGDTYGRV
RRMVDEYGRD VEEAGPSRPV QVQGLNGVPG AGDNLLVVED DRIARQIANQ RNARKRNALA
ARSRKRVSLE DLDSVLKEHS TLNLILKGDN AGSVEALEEA LLKIEMDDEV QLNIIDRGVG
AVTQTNVTLA AASDAVIIAF NVRAEGKATE EANAEGVDVR YYTIIYRAIE EVEAALKGML
KPIYEERVIG HAEIRAIFKA SSVGLIAGCM VEDGKVRRNA TVRITRDGNV IAENAKIVSL
RREKDDATEV SAGYECGMVL SYPDISVDDK IEVYEMVEVP REA
