ID   IF2_AZOSB               Reviewed;         940 AA.
AC   A1K7B9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=azo2107;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM406670; CAL94724.1; -; Genomic_DNA.
DR   RefSeq; WP_011765838.1; NC_008702.1.
DR   AlphaFoldDB; A1K7B9; -.
DR   SMR; A1K7B9; -.
DR   STRING; 62928.azo2107; -.
DR   EnsemblBacteria; CAL94724; CAL94724; azo2107.
DR   KEGG; aoa:dqs_2239; -.
DR   KEGG; azo:azo2107; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_4; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002588; 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; Reference proteome.
FT   CHAIN           1..940
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335458"
FT   DOMAIN          440..609
FT                   /note="tr-type G"
FT   REGION          138..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..456
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          474..478
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          495..498
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          549..552
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          585..587
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        146..162
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         449..456
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         495..499
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         549..552
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   940 AA;  100829 MW;  75C673CB04A9D1B4 CRC64;
     MEQMSVTQFA GELKMPAAAL LEQLKRAGVD KSSAADLLTE QDKSRLLEYL RRAHGGGEPK
     GKITLTRKQT TEIRATDSTG RARTVQVEVR KKRTFVKRDE LLGDAASAES PLLEEELSVA
     GEAAGEAVAA PEPVLEAAPV EVVAEPEPVQ PEPLPEPEPE PVVVEEAPVQ QAAEPEPVEA
     AAVAAEAESP ESAQPAAPRA RPVSITELLS EEEIAARERE ARRHRELVER QQADLRARQQ
     REAAAKAAAE ARRLDEEAKA RAEQQKKEEA AKPAAKPAPG PTGTLHRPAK ADDKAGKDAK
     RGPAREADGA KRRGIKTRGE VGGAASGNAW RGAKGGGRHG RQQDDRQTFQ APTEPIVREV
     HVPETITVAD LAHKMSVKAT EVIKTLMKMG SMVTINQVLD QETAMIVVEE LGHKALAAKL
     DDPDAFLEET DAHKDAELLP RAPVVTVMGH VDHGKTSLLD YIRRAKVAAG EAGGITQHIG
     AYHVETPRGV ITFLDTPGHE AFTAMRARGA KATDIVILVC AADDGVMPQT REAIHHAKAA
     GVPVVVAITK IDKPEANAER VKQELVSESV IPEEYGGDTM FVPVSAKTGT GVDELLEAVL
     LQAEVLELTA AVDAPAKGLI VEARLDKGRG PVASLLVQSG TLRKGDVLLV GATFGRIRAM
     LDENGKPVDE AGPSIPVEIL GLSDVPAAGD EAIVLGDEKK AREIALFRQG KFRDVKLAKQ
     QAAKLESMFE QMAEGEVKSL PLIIKADVQG SQEALAQSLA KLSNDEVRVN VIHGAVGAIS
     ESDVNLAQAS GAVIIGFNTR ADAGARKLAE SFGVDIRYYN IIYDAVDEVK SALSGMLAPE
     KREEVIGMVE IRQVFTISKV GSVAGCYVLE GLVKRGSSVR LIRNHTVVWT GELESLKRFK
     DDVKEVKFGY ECGLQLKNYN DIQVGDQLEV FEIKEVARTL