ID   IF2_DEHMB               Reviewed;         593 AA.
AC   A5FQR6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=DehaBAV1_0874;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS   BAV1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ritalahti K.M., Loeffler F., Richardson P.;
RT   "Complete sequence of Dehalococcoides sp. BAV1.";
RL   Submitted (MAY-2007) 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; CP000688; ABQ17456.1; -; Genomic_DNA.
DR   RefSeq; WP_011309424.1; NC_009455.1.
DR   AlphaFoldDB; A5FQR6; -.
DR   SMR; A5FQR6; -.
DR   KEGG; deb:DehaBAV1_0874; -.
DR   PATRIC; fig|216389.18.peg.924; -.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; NRDNRTG; -.
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; 1.
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.
FT   CHAIN           1..593
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000075603"
FT   DOMAIN          101..270
FT                   /note="tr-type G"
FT   REGION          110..117
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          135..139
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          156..159
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          210..213
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          246..248
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         110..117
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         156..160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         210..213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   593 AA;  64080 MW;  EC0325DC858036F8 CRC64;
     MVEKTSKPSA KTEVAPPVKI IELGAAVSVK ELADSLETNP VEVIKALMRK GIMANINQVI
     DFDIAKGVIE AAGFEAKLKI LKKSAAKKAS PAKEKLSNFP LRPPVVTIMG HVDHGKTRLL
     DAIRSTNVME KEVGGITQHI GAYQVEIKGH KITFLDTPGH EAFTAMRARG AQATDITILV
     VAADDGVMPQ TLEALDHAKA AGVPIILAIN KMDKPEANPD RVKQQLAEVG LVVEEWGGDT
     LAIPTSAREN KGINELLEAV LLIAELEDLR ADPNQPASGV VIEAEMDKTK GPMATVLVQS
     GTLKLGDTVV AGNTWGRVKA MFNDVGKRIK KAEPSTPVAL LGMESVPQVG DKIIAVATEK
     QARDMVNENS QSTRKTNAVS LTNVYDQVSQ GNIKELNIIL KTDVQGSLEP IKDSLEKLST
     DKIKININRS GAGNVTESDV MLAMASGGLI IGFSTGIETN AQRLADAEDI DIRHYDIIYK
     LIEDVDKALQ GLLEPTIKEV IDGRAEVRAV FESTKKLSIA GCMVLEGKLV KNSQVRLLRG
     GEVIVDAPSN SLRRFKEDVK EVVAGYECGV GLKDFNEFQK SDILEFYHKE KSR