ID   IF2_BORBR               Reviewed;         997 AA.
AC   Q7WHG2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BB3246;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640446; CAE33738.1; -; Genomic_DNA.
DR   RefSeq; WP_003810548.1; NC_002927.3.
DR   AlphaFoldDB; Q7WHG2; -.
DR   SMR; Q7WHG2; -.
DR   STRING; 257310.BB3246; -.
DR   PRIDE; Q7WHG2; -.
DR   EnsemblBacteria; CAE33738; CAE33738; BB3246.
DR   GeneID; 56479356; -.
DR   KEGG; bbr:BB3246; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_4; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001027; 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; 2.
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..997
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137173"
FT   DOMAIN          498..665
FT                   /note="tr-type G"
FT   REGION          101..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..514
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          532..536
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          553..556
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          607..610
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          643..645
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        180..194
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         507..514
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         553..557
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         607..610
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   997 AA;  106165 MW;  AA8DA462AE4B47D5 CRC64;
     MSSNTVAQFA TELKMPANVL LEQLRAAGVD LKSVDDAVTD SDKAKLLESL RRAHGATEGK
     KITLTRRQTS EIRQADATGR SRTIQVEVRK KRVFVKRDPA ELAAEQAAAR AEEAAAEAVP
     AEAAPAPAEP VRAEPAVETA AKPVEPPVAE APAEPVAAPA AEPQSEQPAQ AEAQPEPTPA
     AQAEPEPQPE PQPEAAPAQA VAEPVEPAKN VSVTETEAEQ ARPEPVVHAQ TELTSKTPAP
     VAQPSAPAES PKSAKAEPAA APKTTAKPGE IRRAAAPAAP DRAREEARRA AEAEAAALRE
     MLSRPRKVLR APEPEPQAGA LSGTLHKPAG KPATTAAPKK DAKPGAPGAK KTIKTAEVSS
     TWSDDSARKK PADNKPAVTT RDGWRAGGKG GRGGRNSRNQ HQDRRHEQVQ QEFIAREIHV
     PETISVADLA HKMSVKAAEV IKQLMKLGQM VTINQVLDQE TAMIVVQEFG HMAIAAKLDD
     PEAFLDETAA VTEAEAEPRA PVVTVMGHVD HGKTSLLDYI RRAKVASGEA GGITQHIGAY
     HVETGRGVVT FLDTPGHEAF TAMRARGAKA TDIVILVVAA DDGVMPQTRE AIHHAKAGGV
     PLVVAVNKID KPEANPERVK QELVAEEVVP EEYGGDVPFV PVSAKTGAGI DDLLENVLLQ
     AEILELKAPI EAPAKGLVIE ARLDKGRGPV ATILVQSGTL KRGDVVLAGA SFGRVRAMLD
     ENGKQIQTAG PSIPVEIQGL TEVPAAGDEL MVLSDERKAR EIALFRQGKF RDVKLARQQA
     AKLESMFDNL GEGTQTLALI VKTDVQGSQE ALVSSLTKLS TDEVRVQVVH AAVGGISESD
     VNLAIASNAV VIGFNVRAEQ SAKKLAETNG IDLRYYNIIY DAVDEVKAAM SGMLAPEKRE
     EVIGLVEVRE VYTISRIGTV AGCMVLDGVV RRDSQVRLLR NNVVQWTGHL DSLRRFKDDV
     KEVKSGFDCG LTLRGNNDLQ LGDQLEVFEI KEIARTL