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 03-AUG-2022, entry version 77.
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; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
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}.
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; 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 PRIDE; B9M1G0; -.
DR EnsemblBacteria; ACM21042; ACM21042; Geob_2692.
DR KEGG; geo:Geob_2692; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79180at2; -.
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; 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; 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; PF04760; IF2_N; 2.
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..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
