ID   IF2_ALKCK               Reviewed;         761 AA.
AC   Q5WFU2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ABC2228;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD64763.1; -; Genomic_DNA.
DR   RefSeq; WP_011247071.1; NC_006582.1.
DR   AlphaFoldDB; Q5WFU2; -.
DR   SMR; Q5WFU2; -.
DR   STRING; 66692.ABC2228; -.
DR   EnsemblBacteria; BAD64763; BAD64763; ABC2228.
DR   KEGG; bcl:ABC2228; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001168; 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..761
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228165"
FT   DOMAIN          262..435
FT                   /note="tr-type G"
FT   REGION          39..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..278
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          296..300
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          317..320
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          371..374
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          407..409
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        55..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         271..278
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         317..321
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         371..374
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   761 AA;  82736 MW;  74DDE8266BEE39EF CRC64;
     MSKVRIYEYA KANNVQSKQL IESLKSMGVE VSNHMSAIDE ETLNKAKQAG KPAAAKGQGS
     TSNQKQNSQN QRSNQGQKQR PQNNQQNQGQ KQRPQNNQQS QSQGQTKRPS QASNNQSGAA
     KSQAGKPNQN RGGNRPGGQG RPGSNNRRPG NNQNRRNHGN RGGKRRPQSK VNHQQMPLPE
     KITISGSHTV SELAAKLHRE ASELIKKLIG LGVMATINQE LDKDTIELLA ADYGVEVEEE
     VIVDELDIEL YDREDKEEEL KERPPVVTIM GHVDHGKTTL LDSIRNTKVT AGEAGGITQH
     IGAYQIEHSG KKITFLDTPG HAAFTTMRAR GAQVTDITIL VVAADDGVMP QTKEAISHAK
     AAEVPIIVAV NKIDKETASP DRVMQELTEF ELVPEAWGGD TIFVNVSALT GEGIDELIEM
     ILLVAEVEEF KANPDKLATG TVVEAQLDKG RGPVATLLVQ SGTLNVGDAV VVGSTFGRVR
     ALVNDVGRRV KTAGPSAPVE ITGLNEVPQA GDRFQAFEDE KKARQLGEGL MARYREQNLT
     ASSKVSLDDL FNQIQQGDVK DINVIIKADV QGSVEAMKGS LEKIDVAGVK VNIIHTGAGA
     ITESDIILAS ASNAIVIGFN VRPDVNAKRV AEAENVDIRL HRVIYNAIDE IEQAMKGALD
     PEFEEKVIGQ VEVRTTFKVS KVGTIAGSYV TEGKITRNSS VRLIRDGIVI YEGELNALKR
     YKDDAKEVQA GYECGITLDK FNDIKEGDMI EAYVMEEVKR A