IF2_COREF
ID IF2_COREF Reviewed; 964 AA.
AC Q8FPA7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CE1878;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18688.1; -; Genomic_DNA.
DR RefSeq; WP_011075654.1; NC_004369.1.
DR AlphaFoldDB; Q8FPA7; -.
DR SMR; Q8FPA7; -.
DR STRING; 196164.23493719; -.
DR EnsemblBacteria; BAC18688; BAC18688; BAC18688.
DR KEGG; cef:CE1878; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001409; 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; Reference proteome.
FT CHAIN 1..964
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137196"
FT DOMAIN 459..631
FT /note="tr-type G"
FT REGION 35..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..475
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 493..497
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 518..521
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 572..575
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 608..610
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 70..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 468..475
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 518..522
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 572..575
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 964 AA; 100081 MW; AE61FD1A622612F8 CRC64;
MPGKLRVHEL AKKLGITSKE LLATLKEQGE FVKTASSTIE PPVVKKMQEH YQATGGAKPD
TDNKPTPAKP AAKPGAPAPK PGTAQKPTAP TPGAVAAPKP GTAAAKPTPA KPAAPKPTAA
KPAPAKPTAP KPATPAFSGP TPGDAAKKAA EDKATPKPGG EAPRPNAMPR PMAKPGPKPG
ARAPRVANNP FSTGAADRPG PRPGGGGPRP GGGPRPGGAP RPQGGQRSGA PRDGQGGPRG
QRPGPGSGGP RPQGGNAAGA ASQERQGGGR RPSPAMMPPT PGQMPAKAPG KGGRGGGQGG
PGGGSGGFNR GGGGGAGRGG RRGGTAGAFG RPGGAPRRGR KSKRQKRNEY ESMQAPNVIG
GVRLPDGRGQ TLRLARGASL SDFADKIGAD AAALVQALFN LGEMVTATAS VSDETLMLLG
DEMNFKVEVV SPEDEDRELL ESFDLQFGED IGDEQDLAKR PPVVTVMGHV DHGKTRLLDT
IRKANVGSGE AGGITQGIGA YQVKVEVEDD LRTITFLDTP GHEAFTAMRA RGAKSTDIAV
LVVAADDGVM PQTIEAINHA KAADVPIVVA VNKIDKPDAS PEKIRGQLTE YGLVPEEYGG
DTIFVDISAK QGTNIDELLA SVCLTADAEL DLVANPDMDA QGVAIEAHLD RGRGPVATVI
VQRGTLRVGD SIVVGDTYGR VRRMVDEYGR DVDEAGPSRP VQVQGLNGVP GAGDNLLVVE
DDRIARQIAN QRNARKRNAL AARSRKRVSL EDLDSVLKET SVLNLILKGD NAGSVEALEE
ALLKIEMDDE VELNIIDRGV GAVTQTNVTL AAASNAVIIA FNVRAEGKAT EEANAEGVDI
RYYTIIYRAI EEVEAALKGM LKPIYEEREV GKAEIRAIFK ASAIGLIAGC MVEEGKVRRN
ATARIIRDGN VIASNAKIES LRREKDDVTE VSAGYECGMV LSYPDIAVGD KIEVFEMVEV
PRDS
