ID   IF2_STIAU               Reviewed;        1054 AA.
AC   P55875;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Translation initiation factor IF-2;
GN   Name=infB;
OS   Stigmatella aurantiaca.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Archangiaceae; Stigmatella.
OX   NCBI_TaxID=41;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DW4;
RX   PubMed=9079922; DOI=10.1128/jb.179.7.2348-2355.1997;
RA   Bremaud L., Laalami S., Derijard B., Cenatiempo Y.;
RT   "Translation initiation factor IF2 of the myxobacterium Stigmatella
RT   aurantiaca: presence of a single species with an unusual N-terminal
RT   sequence.";
RL   J. Bacteriol. 179:2348-2355(1997).
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; X87940; CAA61162.1; -; Genomic_DNA.
DR   PIR; T43226; T43226.
DR   AlphaFoldDB; P55875; -.
DR   SMR; P55875; -.
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..1054
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137256"
FT   DOMAIN          552..721
FT                   /note="tr-type G"
FT   REGION          57..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..568
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          586..590
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          607..610
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          661..664
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          697..699
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        88..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..424
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         561..568
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         607..611
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         661..664
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1054 AA;  111324 MW;  FFD519530B5D0669 CRC64;
     MSKKRVHEIA KELKGHGIEL DNKEVVTELA GLGYDVKSHS SSLDDDQATA AVQKILDKRK
     PKQAAAPVTA KGFVVRRKVG PPTGSGVYDA SQEPSQAASD VSSPPSEPVH EASGAEAAAS
     ERVPEAAAVQ EPVAEAPRAA ASEPAAEAPK ATAPVAPEPT VEAPKAAAPV APEPTVEAPK
     TEAPVAAAPI AEAPTPPART EVPVTSGRRA ASCRGAAPLP CSGKDPLALN SSPQSSAAFC
     PDARNPGDCD FPSTSGRWHA WPSRGSSGRF AHGAGRPSGW TFARWTSGRP RAASRRTAVQ
     RPSGRAGAGA SHGLQRRKGF GAGAQASGQP QNVTMVGGIP HAPTAPDARA LRPTATQAVV
     ISRPLIQVRR VTPTTSSAKQ YPMAPGKKAI GEVREFKVVP DHAGRGRELV DVSKNKDKSP
     RKRGGPNDTS ISKQELTDLA WGRVNIPLRG KKKKPTKKGA KTQITQMAED KKVIKLQEGI
     SVSDLGQRMG VRTSDIIKKL MGLGKMATAN QMVDADTVEL IASDYGWKVD RVGFEVEDYL
     PEVVARPEDA RTRPPVVTVM GHVDHGKTSL LDAIRAANVA SGEAGGITQH IGAYSVTTAR
     GDITFLDTPG HEAFTSMRAR GANVTDIVIL VVAADDGVMP QTIEAIKHAK AAEVPIVVAL
     NKMDVPGANP DRVKKDLANH ELVPEEWGGE TIMVPVSAKQ KMGIDLLLEN VVLQAEVLEL
     TSNPSRPAVG AIIEGELDRG RGPVATVLVQ EGTLRVGDAV VTGTDYGRVR AMNNSRGESV
     KEVLPGYCAE VIGLSGVPSA GDTINVVADE KAAKQIAEHR GMKERQSELS KVSRETLDQL
     FAKTKAGGGP KELRVVIKAD VQGSAEAVKQ AVQKLTTHKV KVEVIDTGVG AITESDVMRA
     AASKGVVLGF NVKPESGAES AAKAEGVMLR SFSIIYELID GVRSSMEELL EPIRTERKLG
     RAEVRNTFNV PKLGTIAGAA VLDGVIKRGA FVRLMRENKQ LFAGKMASLR RFKDDVKEVA
     QGFECGIGIE NFNDLKAGDI IEAYEIEETR QSLT