ID   IF2_AYWBP               Reviewed;         623 AA.
AC   Q2NIQ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=AYWB_570;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYWB;
RX   PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA   Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to diverse
RT   environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(2006).
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; CP000061; ABC65687.1; -; Genomic_DNA.
DR   RefSeq; WP_011412849.1; NC_007716.1.
DR   AlphaFoldDB; Q2NIQ6; -.
DR   SMR; Q2NIQ6; -.
DR   STRING; 322098.AYWB_570; -.
DR   PRIDE; Q2NIQ6; -.
DR   EnsemblBacteria; ABC65687; ABC65687; AYWB_570.
DR   KEGG; ayw:AYWB_570; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   PhylomeDB; Q2NIQ6; -.
DR   Proteomes; UP000001934; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..623
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008198"
FT   DOMAIN          125..293
FT                   /note="tr-type G"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..141
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          159..163
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          180..183
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          234..237
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          270..272
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         180..184
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         234..237
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   623 AA;  69163 MW;  4F2A0984DA982137 CRC64;
     MTLNKKTNNE NSSKTTPKLS KKTDFQNDFA SKNYVFNPQD KVFQIAQVFG ITSAVLIKKL
     LQLGLKADVN QTLEKDIVEL LAKEYNIKVI EPQKEQTPPQ LQPQKPPLTK SKLQAKPNQK
     LNLQKTPPIV TIMGHVDHGK TTLLDAIRKT RVVDQEFGGI TQHIGAYQVE YQGNKITFID
     TPGHEAFDKM RARGAKITDI CILVVAVDDC VKPQTLEALK HAQKAQIPII VALNKVDKPN
     NKTQQIMQEL SSYDLLPEEW GGTTPYIAIS ALKREGLEKI LEIILLFSEI QNLQTNPDQK
     AKGTVIEASL DKSLGPVATF IISDGNLKVG DIVVAGTSYG KIRSMEDENK KTPTKALPSQ
     PVRVSGLKEV PQAGDIFYAV SNEKQARQIV SEKKTKTKET LAKPPSPLNL EDILQDLETE
     KPQELNIILK ADTQGSLEAL QGMIDKIKVS DLKVQLLRAA VGTITEKDIA FAKSSDSLLI
     GFNIKPAFST LKSAQIQEVK ITIHNVIYRI IEDIEQKLKS MIKPTFEEVV TGKVEVRKIF
     NISKVGNIAG CYVTQGIVNN SDFAKVMRND EVLFKGKITS LKHLKDNIKS AKQGHECGIL
     LDGFNDFEIN DIIETSKLSK VEE