ID   IF2_GEOSW               Reviewed;         732 AA.
AC   C5D9C9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=GWCH70_1155;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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; CP001638; ACS24015.1; -; Genomic_DNA.
DR   RefSeq; WP_015863487.1; NC_012793.1.
DR   AlphaFoldDB; C5D9C9; -.
DR   SMR; C5D9C9; -.
DR   STRING; 471223.GWCH70_1155; -.
DR   EnsemblBacteria; ACS24015; ACS24015; GWCH70_1155.
DR   KEGG; gwc:GWCH70_1155; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
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..732
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000202774"
FT   DOMAIN          233..402
FT                   /note="tr-type G"
FT   REGION          40..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..249
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          267..271
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          288..291
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          342..345
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          378..380
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        40..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         242..249
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         288..292
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         342..345
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   732 AA;  81945 MW;  9A6B0A56EED31CCB CRC64;
     MSKMRVYEYA KKNNVPSKDV IHKLKEMNIE VTNHMATLEP EVVEKLDHTY NKKNERPQAS
     APKEKQKAPV KPKNYVDDFD DEDEEVVKTK VPKKKSANKK KEGKKHDLQL QQQEKKIFHQ
     QKKKIKGKAK AKEQQPVQQE QPMKKEKELP KKITFEGTLT VAELAKKLGR EPSEIIKKLF
     MLGVMATINQ ELDKDAIELI CSDYGVEVEE KVVIDETNFE SIEIVDDPED LVERPPVVTI
     MGHVDHGKTT LLDSIRHSKV TEQEAGGITQ HIGAYQVTVN DKKITFLDTP GHEAFTTMRA
     RGAQVTDIVV LVVAADDGVM PQTVEAINHA KAANVPIIVA INKMDKPDAN PDRVMQELME
     YNLIPEEWGG DTIFCKLSAK TGEGIDNLLE MILLVSEMEE LKANPNRRAT GTVIEAKLDK
     GRGPVATLLV QAGTLHVGDP IVVGCTYGRV RAMVNDTGRR VKEAGPSTPV EITGLHEVPQ
     AGDRFMVFED EKKARQIGEA RAQKQLMEQR NMKARVSLDD LFEQIKQGEM KELNIIVKAD
     VQGSVEALVA ALQKIEVEGV RVKIIHAAVG AITESDILLA TTSNAIVIGF NVRPDANAKR
     VAESEKVDIR LHRIIYKVIE EIEAAMKGML DPEYEEKVIG QAEVRQTFKV SKVGTIAGCY
     VTDGKITRDS KVRLIRQGIV VYEGEIDSLK RFKDDVKEVM QGYECGLTIK NFNDIKEGDV
     IEAYIMQEVE RK