ID   IF2_STRCO               Reviewed;        1033 AA.
AC   Q8CJQ8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SCO5706;
GN   ORFNames=SC5H4.30, SC9F2.10c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939124; CAD55362.1; -; Genomic_DNA.
DR   PIR; T35989; T35989.
DR   RefSeq; NP_733671.1; NC_003888.3.
DR   RefSeq; WP_011030402.1; NZ_VNID01000024.1.
DR   AlphaFoldDB; Q8CJQ8; -.
DR   SMR; Q8CJQ8; -.
DR   STRING; 100226.SCO5706; -.
DR   GeneID; 1101145; -.
DR   KEGG; sco:SCO5706; -.
DR   PATRIC; fig|100226.15.peg.5795; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_9_3_11; -.
DR   InParanoid; Q8CJQ8; -.
DR   OMA; QVRPEMI; -.
DR   PhylomeDB; Q8CJQ8; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1033
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137261"
FT   DOMAIN          526..698
FT                   /note="tr-type G"
FT   REGION          49..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..542
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          560..564
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          585..588
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          639..642
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          675..677
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        110..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..255
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..314
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         535..542
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         585..589
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         639..642
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1033 AA;  105658 MW;  47D581FB0072A045 CRC64;
     MAKVRVYELA KEFGVESKVV MAKLQELGEF VRSASSTIEA PVVRKLTDAF QQGGGNGRSA
     GRPAAPKKAA PRPSAPSPAQ AGPSQAAPAA GDRAAAPRPS AAPKAPAAQQ PAAPSAPAPA
     PSQGPRPTPG PKPAPRPAPA APEFTAPPAA PAAPSTPAPA PSGPKPGGAR PGAPKPGGAR
     PSGPGQDRGQ QGGQGRPGGQ RPGAPAQRPG GRPGGPRPGN NPFTSGGNAG MARPSAPRPQ
     GGPRPGGPGG APGGGPRPQG PGGQGGGPRP QAPGGNRPSP GSMPRPQGGG AGPRPGGGPR
     PNPGMMPQRP AAGPRPGPGG GGRGPGGAGR PGGGGGRPGG GGFAGRPGGG GGGRPGGGGG
     FAGRPGGGGG FGGGGGRPGF GGRPGGPGGR GGTQGAFGRP GGPARRGRKS KRQRRQEYEA
     MQAPSVGGVM LPRGNGETIR LSRGASLTDF AEKINANPAS LVAVMMNLGE MVTATQSVSD
     ETLHLLAGEM NYTVQIVSPE EEDRELLESF DLEFGEDEGS EEDLVVRPPV VTVMGHVDHG
     KTRLLDAIRK TNVIAGEAGG ITQHIGAYQV ATEVNDEERK ITFIDTPGHE AFTAMRARGA
     RSTDIAILVV AANDGVMPQT VEALNHAKAA EVPIVVAVNK IDVEGADPTK VRGQLTEYGL
     VAEEYGGDTM FVDISAKQGL HIDSLLEAVV LTADASLDLR ANPVQDAQGI SIESRLDRGR
     GAVATVLVQR GTLRVGDTMV VGDAYGRVRA MLDDNGNNVA EAGPSTPVQV LGLTNVPGAG
     DNFIVVEEDR TARQIAEKRA ARERNAAFAK RTRRVSLEDL DKVLKAGEVQ QLNLIIKGDA
     SGSVEALESS LLQLDVGEEV DIRVLHRGVG AVTESDIDLA MGSDAIVIGF NVRAAGRAAQ
     MAEREGVDVR YYSVIYQAIE EIEAALKGML KPEYEEVELG TAEIREVFRS SKLGNIAGVL
     IRSGEVKRNT KARLLRDGKV IAENLNIEGL RRFKDDVTEI REGFEGGINL GNFNDIKVDD
     VIATYEMREK PRV