ID   IF2_CLOTE               Reviewed;         685 AA.
AC   Q895J8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CTC_01275;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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}.
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; AE015927; AAO35842.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q895J8; -.
DR   SMR; Q895J8; -.
DR   STRING; 212717.CTC_01275; -.
DR   EnsemblBacteria; AAO35842; AAO35842; CTC_01275.
DR   KEGG; ctc:CTC_01275; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001412; 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..685
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137195"
FT   DOMAIN          185..354
FT                   /note="tr-type G"
FT   REGION          194..201
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          219..223
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          240..243
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          294..297
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          330..332
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..201
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         240..244
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   685 AA;  75657 MW;  44694B4494F00928 CRC64;
     MNALSKVRVY ELSKELGISS KDLISLLKDE FSIEVKNHMS VVEEEDALLI KEFYGESKEE
     NTEENIEEKY GDLQEAQIKV VKKNRKNKVK KNDDENDAQE EIVIEMEDTI TVKELSDRLK
     KTYAEVIKEL MMMGVMAAVN QEIDFEAAEK LGEKFEAIVV QREVDVLEES VEQYIEEEEE
     EGTVKRPPVV TVMGHVDHGK TSLLDAIRKE EVAASEAGGI TQHIGAYTIT INGEKITFLD
     TPGHEAFTSM RARGAQITDI VILVVAADDG IMPQTEEAIN HCKAANVPMV VAINKMDRAG
     ANPDKVKQQL AEKGLVAEDW GGDTITVPVS AHTKEGIDTL LEMVLLTAEM QELKSNPNRK
     AKGTVVDAKL DKGRGPVASL IVQNGTLNSG DSIIVGTTYG RIRAMFDDKG RKINSAGPSI
     PAEILGLSEV PSAGDRFYVV KDEKTAREMA EKRKEKTRSE YLATSKVSLE DLYSQIKEGK
     IKELNIIVKA DVQGTIEAIR QSLEKLSTDE VKVRVIHGGV GAITETDVIL ANASSAVIIG
     FNVRPDSNAI VSAEKENVEI KTYRVIYSAI EDIKKAMIGM LEPEYKEVIQ GRAEVRMTYK
     ISNVGTVAGC YVQSGKITRN SGVRIIRDGI VIFESELSSL KRFKDDAKEV AAGYECGIMV
     EKFNDIKEGD TIEAYTMETI KKHTL