IF2_STRGG
ID IF2_STRGG Reviewed; 1038 AA.
AC B1VYN5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SGR_1811;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG18640.1; -; Genomic_DNA.
DR RefSeq; WP_012378793.1; NC_010572.1.
DR AlphaFoldDB; B1VYN5; -.
DR SMR; B1VYN5; -.
DR STRING; 455632.SGR_1811; -.
DR EnsemblBacteria; BAG18640; BAG18640; SGR_1811.
DR GeneID; 31221076; -.
DR KEGG; sgr:SGR_1811; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000001685; 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..1038
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093828"
FT DOMAIN 531..703
FT /note="tr-type G"
FT REGION 48..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..547
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 565..569
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 590..593
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 644..647
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 680..682
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 82..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 540..547
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 590..594
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 644..647
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1038 AA; 106008 MW; 04662EE76FF59B44 CRC64;
MAKVRVYELA KEFGVESKVV MAKLQELGEF VRSASSTIEA PVVRKLTDAL QGPGGNAGKS
AAKPGAPRKA APAKPAAPSP AAAARPAAPK PGAPAPKPAE APSSTPAAPS APSAGPRPGP
KPAPKAAPVT PVPAAEFSAP APAQPAAPQP QAPRPAGATP GPRPTPARPA PAGGQRDGGR
DGGQRDGGRG GERGGDRPAR PAGQGAPRPG GARPAGPRPG NNPFTSGGST GMARPSAPRP
GGAPRPGGGQ ERPGAPRPQG SGPGGAPRPQ GGQGQGGARP TPGGMPRPQA PRPGGGPAGN
RPNPGMMPQR PAAGPRPGPG GGGRGPGGGG RPGAGGGGRP GGGGFAGRPG GGGGGGFAGR
PAGPGGGGGA GRPGGGGGFG GRPGFGGRPG GPGGRGGTQG AFGRPGGPAR RGRKSKRQRR
QEYEAMQAPS VGGVMLPRGN GQAVRLSRGA SLTDFAEKIN ANPASLVAVM MNLGEMVTAT
QSVSDETLRL LAEEMNYVLE IVSPEEEDRE LLESFDIEFG EDEGGEEALV SRPPVVTVMG
HVDHGKTRLL DAIRKTNVVA GEAGGITQHI GAYQVSSEVN GEDRKITFID TPGHEAFTAM
RARGAKSTDI AILVVAANDG VMPQTIEALN HAKAAEVPIV VAVNKIDVEG ADPTKVRGQL
TEFGLVAEEY GGDTMFVDIS AKQGLNIEAL LEAVVLTADA SLDLRANPEQ DAQGIAIESH
LDRGRGAVST VLVQRGTLRI GDTVVVGDAY GRVRAMLDDN GQNVQEAGPS TPVLVLGLTN
VPGAGDNLLV VDEDRTARQI AEKRAARERN ANFARKGVRF SLENLDEALK AGLVQELNLI
IKGDASGSVE ALESSLLQLD VGEEVDIRIL HRGVGAVTES DINLATGSDA IVIGFNVRAA
GRAEQMAERE GVDVRYYSVI YQAIEEIEAA LKGLLKPEYE EVELGTAEIR EIFRSSKLGN
IAGVLVRSGE VKRNTKARLL RDGKVIAENL NISGLRRFKD DVTEIREGFE GGINLGNFND
IKIDDVIATY EMREKPRG
