ID   IF2_XYLFM               Reviewed;         892 AA.
AC   B0U1Q8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Xfasm12_0203;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA11236.1; -; Genomic_DNA.
DR   RefSeq; WP_004086265.1; NC_010513.1.
DR   AlphaFoldDB; B0U1Q8; -.
DR   SMR; B0U1Q8; -.
DR   KEGG; xfm:Xfasm12_0203; -.
DR   HOGENOM; CLU_006301_6_1_6; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
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; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF46955; SSF46955; 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.
FT   CHAIN           1..892
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093846"
FT   DOMAIN          391..560
FT                   /note="tr-type G"
FT   REGION          144..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         400..407
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         446..450
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         500..503
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   892 AA;  97250 MW;  D12CC7F901D86D14 CRC64;
     MSQQTTIRKL AELVNTPVEK LLEQLAGAGM KFSGPDQVVT STEKMKLLGF LRRTHGKSDV
     SVGTVREAPK KITLNRRRLQ EVTVNAGRNK TTVNVEVRQK RTYVKTPESE YHTPTKPPIE
     LADAERVEIL RKLEESRQRN LAEQQRLAEV DRQRVEEQER KRREEEQAEL ERQKTESRVV
     EEILVKTDSN SVKPVSKPIS EERTRALPRT VRPTPAARPS VSRSDDRNSN GGVRHKPRGS
     HVIVSDEDDS ARRFVGQMHL TAAERARRGS NTRGKGGGSH RGATHRGNEN SIRSSGAHGF
     ERPTVAVVRE VAVGDTITVA DLAQKLALKS GDMVKALFKM GVMVTITQTI DHDTAVLVSE
     ELGHKVTRAS SSDFEDALLA HTEEVHGEPV PRPPVVTIMG HVDHGKTSLL DYIRRTKIAV
     GEAGGITQHI GAYHVETPRG VISFLDTPGH AAFTSMRARG AKITDIVVLV VAADDGVMPQ
     TKEAVQHARA AGVPLIVAVS KIDKSTADPQ RVKNELLTES VVAEEFGGDT QFVELSAKTG
     VGVDALLDAI SIQAEVLELK AVIEGRATGT VIESSLDKGR GPVATVLVQQ GRLKKGDYLV
     CGTHYGRVRA LFDEVGHQPL AASPSIPVQV LGLSGVPDAG DDFVVVDDER LAKDVAQQRE
     AKRRESRLVT SAGNRMEDIL AQMGKGENQQ VLNLLIKADV QGSLEALKQA LVALSNDDIR
     INVIHVGVGG ITESDANSAV TSKATVIGFN VRADASARKI IEANGVDLRY FSIIYDVIDQ
     VKQVASGLLG VEIREEIIGV AEVRDVFRSS KFGAVAGCMI IEGVVKRSKP IRVLRDNTVV
     FEGELESLRR FKENVDEVRN STECGIGVKA YNDVRVGDSI ECFERIEVAR TL