ID   IF2_CLONN               Reviewed;         683 AA.
AC   A0Q0Q7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NT01CX_2136;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000382; ABK62071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0Q0Q7; -.
DR   SMR; A0Q0Q7; -.
DR   STRING; 386415.NT01CX_2136; -.
DR   EnsemblBacteria; ABK62071; ABK62071; NT01CX_2136.
DR   KEGG; cno:NT01CX_2136; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000008220; 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; Reference proteome.
FT   CHAIN           1..683
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000057652"
FT   DOMAIN          182..351
FT                   /note="tr-type G"
FT   REGION          191..198
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          216..220
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          237..240
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          291..294
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          327..329
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..198
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         237..241
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         291..294
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   683 AA;  75060 MW;  556B9B645B119FA7 CRC64;
     MNVLAKTRVY ELAKELDITS RELIDILASE FNITVKNHMS VLDEEDAELI KEIFDDEENS
     DEKANRSVVA DEEIDASNKK VKNKKKEVKK GNKNADNESS EEEIVIEMED TITVKALADK
     LKKPTTEVIK QLMFMGVMAA INQELDFNTA EKLAEKFNAV IMQKEDDTIT KEIEDEDEGT
     EKRPPVVTVM GHVDHGKTSI LDAIRKAKVT STEAGGITQH IGAYTVNVNG EKITFLDTPG
     HEAFTTMRAR GAQVTDIVIL VVAADDGIMP QTIEAINHCK AAEVPMIVAI NKIDKPAANL
     DRVKQELTEH NLIPEDWGGD VITVPVSAHT KEGLDTLLEM IILTAEMEEL KADPERKAKG
     TVIEAKLDKG RGPVASLLVQ NGTLKVGDSI IVGNTYGRIR AMFDDKGKNI KVAGPSIPVE
     ILGLSEVPDA GDRFNVVKDE KTARNMADKR KEKLREKRMQ STNKVSLEDL YNQIQEGKVK
     ELDVIVKADV QGSVEAVIQS LEKLSTDSVK VRVIHGAVGA ISETDVTLAA ASNAVIIGFN
     VRPSNNATVL AEKEGVNVRT YRVIYDALDD IKAAMVGMLE PEYKEVVLGS AEVRVVYKIS
     SVGTIAGCYV LNGKITRDSS VRVIRDGIVI FESEISSLKR FKDDAKEVAK GYECGLSVEK
     FNDIKEGDII EAFTMEEIKP KNL