ID   IF2_THEMA               Reviewed;         690 AA.
AC   Q9WZN3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Translation initiation factor IF-2;
GN   Name=infB; OrderedLocusNames=TM_0775;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000512; AAD35857.1; -; Genomic_DNA.
DR   PIR; E72337; E72337.
DR   RefSeq; NP_228584.1; NC_000853.1.
DR   RefSeq; WP_004080913.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WZN3; -.
DR   SMR; Q9WZN3; -.
DR   STRING; 243274.THEMA_00775; -.
DR   EnsemblBacteria; AAD35857; AAD35857; TM_0775.
DR   KEGG; tma:TM0775; -.
DR   eggNOG; COG0532; Bacteria.
DR   InParanoid; Q9WZN3; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..690
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137272"
FT   DOMAIN          178..346
FT                   /note="tr-type G"
FT   REGION          187..194
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          212..216
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          233..236
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          287..290
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          324..326
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         233..237
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         287..290
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   690 AA;  77774 MW;  8673FFFA20C37B60 CRC64;
     MARLRVYELA RKLNMSPKEL LQELEELGVN VKSHMSYVDE EMANIIIDLL EEDNRKAKQP
     SKPKKEKGEE EVEKEVVEKK KKKKITLKPD ELKLDIIAEK IGVPQNKIIQ DMFVKRGIAL
     RPGQILKLEE VEQILKEYKI EIEIEEEQQT SVEEVDEFEL LEKRYQELYE KEKDKLVPRP
     PVVTVMGHVD HGKTTLLDRI RSTRVAEREE GGITQSIGAY QVEVNGKKIT FIDTPGHELF
     TEMRARGAQA TDIVVLVVAA DDGVMPQTIE AYNHAKAANV PIIVAINKID KPNANVEKTK
     QELVEKLGLI PEEWGGDTIV VPISARTGQG VDELLEMILL VAEMNEIKCY PEGPARAVII
     ESKLDKKMGP VASAIVKDGV LKVGDAVVAS NTYGRVRNLF DDNMRPIREA YPSQPVMILG
     FEDVPDVHSN VYVVESAEKA KEIVEKRLQR LEAQKQSRKH INLEELMKMM QEKEKKVLNL
     ILKADTYGSV AALKNAINKL QSKEIELNIV HAGVGEISTS DVMLAAAVDG VILGFRVKVN
     NQARRLAEQE GVDVRTYSII YKLVEDLKLA LEGMLEPEEV EEVIGHGEIR KVFKISKVGK
     VAGVQMLDGK ADRNGFVRIY RNGQLVFGGK IESLKHYKED VSVVEAPQEC GIKFAGFDDI
     HEGDELEFYV IRKVKRKPTF VEEQADQEQK