ID   IF2_BLOPB               Reviewed;         891 AA.
AC   Q493T7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BPEN_108;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40748.1; -; Genomic_DNA.
DR   RefSeq; WP_011282655.1; NC_007292.1.
DR   AlphaFoldDB; Q493T7; -.
DR   SMR; Q493T7; -.
DR   STRING; 291272.BPEN_108; -.
DR   EnsemblBacteria; AAZ40748; AAZ40748; BPEN_108.
DR   KEGG; bpn:BPEN_108; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   BioCyc; CBLO291272:BPEN_RS00525-MON; -.
DR   Proteomes; UP000007794; 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..891
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228173"
FT   DOMAIN          390..559
FT                   /note="tr-type G"
FT   REGION          399..406
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          424..428
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          445..448
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          499..502
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          535..537
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         399..406
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         445..449
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         499..502
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   891 AA;  99368 MW;  E6FC5A31F94F22E3 CRC64;
     MTDTTIQSFA AEMKMSVDQL IQWFSYIGIL KTEIGIVTQR EKEILFKYMN DNKSDISKKL
     ILQRKTRSIL SVSSVGGKNK KVQIEIRKKL TYVQSTLQET EFIDVKNKMV LDANREASSL
     IVRNNRLVNK KISNTLGPSS LTKISKKNHR YSELIEHKEK VIGKISRKFE DKSLQDSDET
     QLLKKKTKNC WDIELNNTNA ISSNLGDSSS NSKLYCMPEL LEKNNNQKLE NERRNRSRVR
     TRYRNGGKLT KQHKRGNHHR LYEATSDEFG MEEELYIPNR VNKSKRKQSA LVQVFNKPVQ
     TITRDIIIGQ TISVAELANK MSIKSSRVIK TMMQLGIIAT INQIIDQDTA QLVAEEMGHN
     VILRRENELE ELIMNDRDID ITSSDTTLAN RAPIVTIMGH VDHGKTSLLD RIRSTKIASS
     EVGGITQSIG AYHVSTDNGM ITFLDTPGHA AFTAMRARGV QITDIVVLVV AADDGVMPQT
     IEAIEHIKAA NVPVVVAINK IDKSEANPER IKNDLNNHGL IPEEWGGDTQ FIHVSATSGN
     GIDNLLDAIL LQSDMLELKV VHHGMARAIV IESFLDKGRG PVVAVLVREG TLKCGDIILC
     GTEYGRVRAM RNEFGHEITS AGPSIPVELL GLSGSPASGE SVIVVRNEKK AREVALYRQG
     KSREIKLARQ KEPNIENIFS SIKNTSVVSE LNLIVKSDTK GSSEAIRESL ENLSTGGDVT
     IKILSSSIGG ITETDVALAA ASNAVIVGFN VRADPTARRI IEADQLDVRY YSVIYDLIDE
     VKQAVHGMLA PRYKHEIIGL AKVRNVFRSP KYGNVAGCMV VEGMIKRYKK IRVIRDNIVV
     HEGELESLRR FKDDVNEVRS GIECGIGIKN YKNIHSGDMI EVFDMVKISH V