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Database: UniProt
Entry: IF2_GEODF
LinkDB: IF2_GEODF
Original site: IF2_GEODF 
ID   IF2_GEODF               Reviewed;         908 AA.
AC   B9M1G0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Geob_2692;
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) 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; CP001390; ACM21042.1; -; Genomic_DNA.
DR   RefSeq; WP_012647770.1; NC_011979.1.
DR   AlphaFoldDB; B9M1G0; -.
DR   SMR; B9M1G0; -.
DR   STRING; 316067.Geob_2692; -.
DR   KEGG; geo:Geob_2692; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_7; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000007721; 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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
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..908
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000118763"
FT   DOMAIN          408..577
FT                   /note="tr-type G"
FT   REGION          145..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..424
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          442..446
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          463..466
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          517..520
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          553..555
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        249..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         417..424
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         463..467
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         517..520
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   908 AA;  98705 MW;  3AC38D5285300264 CRC64;
     MSKTRVYELA QQMGIDNKEL MAKLAAVGVE VKNHMAAIDD ADIKKLSAPA TVKEVSQEEV
     RVKPTLIRRR AKVVEAVAEE PPVEPKAEPA PAEVTTEKVA EKARVEEAPA PEAPVQAAEP
     VKIATEEAVP ERATANKAKI LGRVEIPGLT QRAKPPVQRE AQPTARVVER PEARPSAERP
     APGQRPEGQR PGQRPEGGYR PAGPRPAGQR PEGPRPGYTE RPVTRGPERP GQARGPERPA
     PVVPLEMPPA GEDRRKGRKG KEVAGAGKKG PAGAAVPKRK EEFKKTELFE KHERVFEPGP
     RGKGKKRQAE KIQIGKKTEI TVPKAIKRII KISETITVGE LAKRMGIKAN DLIRALMKMG
     VMATINHALD FDTATILATD FGYEIENVAL DIDEILESTP DTPESLVKRP PVVTIMGHVD
     HGKTSLLDAI RQTNVIAGEA GGITQHIGAY DVTLNGRKIT FLDTPGHEAF TAMRARGAKV
     TDIVILVVAA DDGVMPQTRE AVNHSKAAGV PIIVAVNKID KPEAKPERVK QELMELGLVS
     EEWGGETIFV DVSAKKRVNL PTLLEMVLLQ ADVLELKANE DKAARGTIVE AKLDKGRGPV
     ATVLVQEGTL KVGDYFVAGI HFGRVRAMQN DRAEKVLSAG PSMPVEVIGF TGVPDAGDVF
     VALADEKQAK EIASLRQQKV RETELAKHSK LSLEQLYEKI QMGEVKDLNT IVKGDVQGSV
     EAVSESLRKL STDAIRLNVI HASVGAITET DVNLATASNA IILGFNVRPE VKAQALAEKE
     GVDIRLYNII YDAVDDIKKA MEGLLEPTLR EKFLGRAEVR ETFSVPKHGT VAGSYVLDGK
     MIRNSQVRLL RDNVVVFEGK MGSLRRFKDD VKEVASGYEC GISIENYNDI KVGDIIESFE
     MEKVATKL
//
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