ID   IF2_BUCA5               Reviewed;         864 AA.
AC   B8D9G2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BUAP5A_370;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=563178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5A;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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; CP001161; ACL30733.1; -; Genomic_DNA.
DR   RefSeq; WP_009874335.1; NC_011833.1.
DR   AlphaFoldDB; B8D9G2; -.
DR   SMR; B8D9G2; -.
DR   PRIDE; B8D9G2; -.
DR   KEGG; bap:BUAP5A_370; -.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; VIFAMNK; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000006904; 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; 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..864
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000118752"
FT   DOMAIN          364..533
FT                   /note="tr-type G"
FT   REGION          140..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..380
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          398..402
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          419..422
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          473..476
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          509..511
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         373..380
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         419..423
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         473..476
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   864 AA;  97518 MW;  55031AFEBCDC9F3C CRC64;
     MPDISLKVLS NEIKISIQEL IKELSIIGIT KTEDNYINVL EKNILLKHLE SKKKYSLDTL
     VLQRKTRSTL RISTVGGKNK SVQVEVRKKR AYVKNNKFEN ESFLNEKKVI KHSMQKTSSL
     KNKEKKYIKN IEKIELNKSD SRSLNTKKEN KLKISNKDEQ NKKFNQHRES NSFDLNHKKR
     IKENKDIRIS HKEEKQDYHL TTFLHARQAE DENDREVEID KRNHGRILKN YRQKKNNKNF
     HNGRYNKEEI RTFNRNKKNS KQKNKPILLQ QVFQKPESII NRDVIISNTI TVSDLANKMA
     IKSSEVIKNM MNMGIIGTIN HVLDQDTAQL IAEEMGHKVI VHRENALEEL IMKDRDTGND
     VSAIRAPVVT IMGHVDHGKT SLLDYIRSTK TAFYEAGGIT QNIGAYHVKT DLGSITFLDT
     PGHSAFTAMR SRGVQITDIV ILVVAADDGV MPQTIEAIQH AKEANVPVIV AINKIDKTDS
     DIDKVRNDLM KYNILSEEWG GENIFVSVSA KTGKGINKLL NVILLQAEML ELKAVTTGMA
     EGIVVESFLD KGRGPIATVL VKKGQLKKGD VILCGFEYGR IKSLRDASGN EVFSAGPSIP
     VEVLGLSKVP FSGDVVTVVR DEKKAREVAS YRKEKSREKK LSNQNRINLE NMFDDINKNN
     VSELKIILKS DIQGSLEAIS GALLKLSTEE VKIKIIGLGI GGITETDASL ALASNAIILG
     FNVRADTSAK KIINSEHLDL RYYSVIYDLL DEVKAAMTGL LSPEYKENII GLAEVRNTFK
     SPKFGLIAGC MVTEGVIKRS NPIHILRNNI VIYEGELESL RRFKEDVNEI RNGLECGIGI
     KNYNDIRVGD IIEVFEVREM KRIL