ID   IF2_ANOFW               Reviewed;         723 AA.
AC   B7GG75;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Aflv_1695;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(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}.
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DR   EMBL; CP000922; ACJ34056.1; -; Genomic_DNA.
DR   RefSeq; WP_012575270.1; NC_011567.1.
DR   AlphaFoldDB; B7GG75; -.
DR   SMR; B7GG75; -.
DR   STRING; 491915.Aflv_1695; -.
DR   EnsemblBacteria; ACJ34056; ACJ34056; Aflv_1695.
DR   KEGG; afl:Aflv_1695; -.
DR   PATRIC; fig|491915.6.peg.1744; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000742; 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..723
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000117319"
FT   DOMAIN          224..393
FT                   /note="tr-type G"
FT   REGION          112..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..240
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          258..262
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          279..282
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          333..336
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          369..371
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         233..240
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         279..283
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         333..336
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   723 AA;  80796 MW;  F3AF6F179E670B92 CRC64;
     MSKMRVYEYA KKHNVSSKDV IHKLKEMNID VSNHMTMIEA DVVEQLDRSF SKEQKQELKK
     EEKKAPVKTP VLEQFEEDED EVIQTKVPIK KAVVKNREGK KHDLQIQQKE KKIFNNKKNK
     KQKPQQAPQQ EVQKKKEKEL PKKITFEGSL TVAELAKKLG KEPSEIIKKL FMLGIIATIN
     KDLDKDAIEL ICSDYGVEVE EKVTIDETEF ETIEIVDNPE DLVERPPVVT IMGHVDHGKT
     TLLDSIRQTK VTEQEAGGIT QHIGAYQVVV NGKKITFLDT PGHEAFTTMR ARGAQVTDIV
     ILVVAADDGV MPQTVEAINH AKAAKVPIIV AVNKIDKPTA NPDRVMQELM EYELVPEEWG
     GDTIYCKLSA LTGEGIDNLL EMILLVSEME ELKANPNRRA TGTVIEAKLD KGRGPVATLL
     VQSGTLRVGD PIVVGYTYGR VRAMTNDLGR RVKEAGPSTP VEITGLNEVP QAGDRFMVFE
     DEKKARQIGE ARAQKQIVQQ RSVKARVSLD DLFEKIKQGE MKELNIIVKA DVQGSVEALV
     AALQKIEVEG VRVKIIHSGV GAVTEYDIML ASASNAIVIG FNVRPDANAK RVAEAEKVDI
     RLHRIIYKVI EEIEAAMKGM LDPEYEEKVI GQAEVRQTFK VSKVGTIAGC YVTDGKITRD
     SSVRLIRQGI VVYEGQIDTL KRYKDDVKEV AQGYECGITI KNFNDIKEGD VIEAYVMQEV
     ARK