ID   IF2_BACVZ               Reviewed;         716 AA.
AC   A7Z4T4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RBAM_016470;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS74010.1; -; Genomic_DNA.
DR   RefSeq; WP_007611462.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4T4; -.
DR   SMR; A7Z4T4; -.
DR   STRING; 326423.RBAM_016470; -.
DR   EnsemblBacteria; ABS74010; ABS74010; RBAM_016470.
DR   KEGG; bay:RBAM_016470; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001120; 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.
FT   CHAIN           1..716
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008199"
FT   DOMAIN          217..386
FT                   /note="tr-type G"
FT   REGION          53..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..233
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          251..255
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          272..275
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          326..329
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          362..364
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        59..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         226..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         272..276
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         326..329
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   716 AA;  78596 MW;  AE5C3487F9A59A47 CRC64;
     MAKMRVYEYA KAINVSSKEI LTALKNMDIV VNNHMAMLEE KTIKQLDAKF KKGGAGVTSQ
     KPAETNKNKP QGINQQPAGN QPNKIRDGKK NDVQNNQFNK NKKNNNNNKN KNKRNHNNKN
     QYQQKPLKPK KELPEKITFS GSLTVGALAE ELGKEPSELI KKLMLLGVMA TINQELDKDT
     IELIASEYGV ETEEVIVLEE TELEKYEEAD KEEDLQIRPP VVTIMGHVDH GKTTLLDSIR
     KTKVVEGEAG GITQHIGAYQ IEENGKKITF LDTPGHAAFT TMRARGAEVT DITILVVAAD
     DGVMPQTVEA INHAKAAEVP IIVAVNKVDK ESANPDRVMQ ELTEYGLVPE AWGGETIFVP
     LSALTGKGID ELVEMILLVS EVEELKANPN RQAKGTVIEA ELDKGRGSVA TLLVQTGTLN
     VGDPIVVGNT FGRVRAMVND LGRRVKTAGP STPVEITGLN DVPQAGDQFL VFKDEKTARS
     VGEARASKQL EEQRSDKAKL SLDDLFEQIK QGDVKDINLI VKADVQGSAE ALTAALQKIE
     VEGVKVKIIH TGVGAITESD IILASASNAI VIGFNVRPDG NAKSTAEAEN VDIRLHRIIY
     KVIEEIEAAM KGMLDPEYEE KVIGQVEVRQ TFKVSKIGTI AGGYVTDGHI TRDSGLRLIR
     DGVVIFEGEV DVLKRFKDDV KEVSQGYECG ITIKKYNDIR EGDIIEAYVM QEIERK