ID   IF2_CLOK5               Reviewed;         694 AA.
AC   A5N842;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CKL_1431;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(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}.
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; CP000673; EDK33473.1; -; Genomic_DNA.
DR   RefSeq; WP_012101820.1; NC_009706.1.
DR   AlphaFoldDB; A5N842; -.
DR   SMR; A5N842; -.
DR   STRING; 431943.CKL_1431; -.
DR   EnsemblBacteria; EDK33473; EDK33473; CKL_1431.
DR   KEGG; ckl:CKL_1431; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002411; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..694
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000075599"
FT   DOMAIN          193..362
FT                   /note="tr-type G"
FT   REGION          202..209
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          227..231
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          248..251
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          302..305
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          338..340
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         248..252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         302..305
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   694 AA;  76853 MW;  37E84F67A7BB9502 CRC64;
     MSKIRIYELA KELNISSKKL ITLLLEEFGV EVKNHMSVIE EEDADLIKEF IEENEDKEEY
     LEDKYKNLPE EKSEKFKKNA GNTVKIADKN KSKQDKAVKD LNEQVSKENH KVEIEDTITV
     KEFSEKIGKP ITEVIKQLIF MGVMAAINQE IDFSTAEKLG EKFDITVLKK KEDIDKGVAE
     QDEDEDEDTN VEKRPPVVTV MGHVDHGKTS LLDAIRKSKV TATEAGGITQ HIGAYTVTIN
     GEKITFLDTP GHEAFTAMRA RGAQITDIVI LVVAADDGIM PQTAEAINHC KAANVPIVVA
     INKIDRPGAN VDKVKQELTE YQLVPEDWGG DTICIPVSAH TKEGIDTLLE MVLLTAEMQE
     LKANSNRNGK GTVVEAKLDK GRGAVATLLI QNGTLSVGDS IIVGSTYGRI RAMFDDKGNK
     IKSAGPSIPV EILGLSEVPA AGDRFHQVKD EKTARDIAEK RKQKIREEYL QSTHKVSLED
     LYNQIKEGKV KELNIIVKAD VQGSIEALKQ SLQKLSNEEV KVRVIHGAVG AITETDVTLA
     SASNAIIIGF NVRPDSNAQA AAEKESVDVK TYRVIYNAIE DIKAAMVGML EPDYKEVILG
     KAEIRQIYKI SNIGTIAGCY VQEGKMVRNC KVRIIRDGIV IFESELASLK RFKDDVKEAA
     EGYECGLSIE KFNDIKEGDI VEAYDIEEIK KKEL