ID   IF2_ALBFT               Reviewed;         978 AA.
AC   Q21WJ5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Rfer_2134;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD69858.1; -; Genomic_DNA.
DR   RefSeq; WP_011464426.1; NC_007908.1.
DR   AlphaFoldDB; Q21WJ5; -.
DR   SMR; Q21WJ5; -.
DR   STRING; 338969.Rfer_2134; -.
DR   PRIDE; Q21WJ5; -.
DR   EnsemblBacteria; ABD69858; ABD69858; Rfer_2134.
DR   KEGG; rfr:Rfer_2134; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_4; -.
DR   OMA; RDVMMAG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000008332; 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..978
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008313"
FT   DOMAIN          478..647
FT                   /note="tr-type G"
FT   REGION          107..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..494
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          512..516
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          533..536
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          587..590
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          623..625
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        146..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         487..494
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         533..537
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         587..590
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   978 AA;  105183 MW;  A0FB3EB46A83A065 CRC64;
     MFSTTVAEFA NELKKSTATL LEQLKSAGVA KTAASDKLND ADKQRLLSYL QSTHGAAGAE
     RKKITLVKKS TTEIKQADAS GKARTIQVEV RKKRTFIRRD DGVEVSAEAP ALETEQEVEA
     APQVDNLELA RREEEARRQA ELIRRQEEEL SERRRQREEQ EARSREASEK AAAVAAEAAE
     AAAAQALKKK SKPVAPEQPA PNPTEIETAK VLAAAEKEQH LAKEKGLARE KELAESKARA
     AEDVVRAADL GDRRRKAESE AAAIRLMMSS PAKKAPPPPK KPEEVKPAMK GTLHKPAAGA
     VPAKPAKPGA PGAPGAPAAG AAAGAGKEVK SAKLSSSWAG DPAKKKGIPT RGATAAPGAG
     RSTNWRAPAR GGRRGSSDRD RDDHRVQAAP VEQRVIEVHV PETITVAELA HKMAVKASEV
     IKHLMKLGQM VTINQPLDQD TAMILVEEMG HKAIVAALDD PEAFTVDEVS QQQSESLPRA
     PVVTVMGHVD HGKTSLLDYI RRAKVATGEA GGITQHIGAY HVETDRGMIS FLDTPGHEAF
     TAMRARGAKA TDIVILVVAA DDGVMPQTKE AIKHARAAGV PIVVAINKID KPDANPERVK
     NELVVEEVVP EEFGGDSPFV PVSAKTGQGI DALLEQVLLQ AEVLELKAPV DAMAKGLVIE
     AQLDKGRGPV ATVLVQSGTL KTGDIVLAGS TYGRVRAMLD ENGRTIKTAG PSIPVEIQGL
     TEVPQAGDEF MVMADERRAR EIATYRAGKF RHTKLAKQQA AKLENMFTDM AAGEVKMVPI
     IIKADVQGSQ EALAQSLLKL STDEVKVQLV YTAVGAISES DVNLAIASKA VIIGFNTRAD
     AGARKLAENN GVDIRYYDII YDAVDELKLA MSGMLTPDKK EEVIGTAEIR QIFKVSKIGS
     IAGCMVTAGV VRRTARLRLL RDNMVIFTGE LDSLKRFKDD VREVREGFDC GLNIKNYNDI
     QEGDVLEFFE IREVARTL