ID   IF2_RUTMC               Reviewed;         815 AA.
AC   A1AV99;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Rmag_0054;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(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; CP000488; ABL01856.1; -; Genomic_DNA.
DR   RefSeq; WP_011737482.1; NC_008610.1.
DR   AlphaFoldDB; A1AV99; -.
DR   SMR; A1AV99; -.
DR   STRING; 413404.Rmag_0054; -.
DR   EnsemblBacteria; ABL01856; ABL01856; Rmag_0054.
DR   KEGG; rma:Rmag_0054; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_1_6; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 139681at2; -.
DR   Proteomes; UP000002587; 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; 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.
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..815
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335507"
FT   DOMAIN          315..482
FT                   /note="tr-type G"
FT   REGION          324..331
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          349..353
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          370..373
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          424..427
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          460..462
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         324..331
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         370..374
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         424..427
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   815 AA;  88783 MW;  B09F1129A4840082 CRC64;
     MAHTVQTLSK LLKKTPDEVI TILANAGVDG KNSDSAISAE ERKILMSSLS KRSSSKSSMF
     SFSKTGIKSS ANSASGAKVQ VKKKRLTKSA TATDEQPEIA VNEVAQAVQV ALDAGRDADK
     KLLAQDAKRL EMVRLQKTQA EVLKAQKKTV KQAQAQEIEK KAEKPKMIDK FKEDKKPKRL
     RNTLNGNNTR RQLHVARHNP NRKLKKKDRT RLSQKVQEEQ AQHAFQKPIE KVVHEIAIAE
     NIKVTELAQK MATKAGEVLK VLMGMGVMAT LNDVIDQDTA MLVVEEMGHK SIASVEETVE
     DVLIEQLKSS GNEKARPPVV TIMGHVDHGK TSLLDYIRQA KVTHGEAGGI TQHIGAYQVQ
     SNGNTITFID TPGHAAFSKM RSRSANATDI VILVVAADDG VMPQTIESIK HVQTAGVPMI
     VAINKIDKEG IDIDKIKQVL STHNVISEDW GGDVMMIPVS AYTGEGVDAL LDAISLTAEV
     LEFSAVIKAL ARGTVLEARL EKGRGKVTTI LVQSGTLNKG DIMIAGFEYG KVKQIVDDKG
     KVLKSATPSM PVEVLGLSGV PNSGDEVLVV DSERKAREVA DFRKAKNREA QLQKQQASKM
     ENFLMKMEES NVSTVNVLLK ADVRGSAQAL IEALEGLSTD EAKVKVVSSG VGGINNTDIT
     LAATSNALVL GFNVRADAVA RKTADNEGVR IEYYSIIYNL IDDVKTIMSG LLSPELSENI
     IGIASVKSVF RSQKMGDIAG CMVEEGVVRR DSLIRVLRDS VVIFEGWLES LRRFKDNVNE
     VKSGTECGIG VLNYTDIQPG DQIEVFERIE RIRTL